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(9Z,12Z,15Z,18Z,21Z)-tetracosa-9,12,15,18,21-pentaenoic acid + AH2 + O2
(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosa-6,9,12,15,18,21-hexaenoic acid + A + H2O
-
-
-
-
?
24-carbon fatty acid + AH2 + O2
? + A + H2O
alpha-linolenic acid + AH2 + O2
(6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid + A + 2 H2O
preferred substrate
-
-
?
alpha-linolenic acid + AH2 + O2
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
alpha-linolenic acid + AH2 + O2
octadeca-6,9,12,15-tetraenoic acid + A + 2 H2O
-
-
-
?
alpha-linolenic acid + AH2 + O2
octadecatetraenoic acid + A + 2 H2O
-
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
alpha-linoleoyl-CoA + AH2 + O2
stearidonoyl-CoA + A + 2 H2O
gamma-linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
39% conversion efficiency
-
-
?
gamma-linolenic acid + AH2 + O2
cis-6,9,12,15-octadecatetraenoic acid + A + H2O
-
-
-
-
?
gamma-linolenic acid methyl ester + O2
?
heptadec-9-enoic acid + AH2 + O2
heptadec-6,9-dienoic acid + A + H2O
-
conversion rate is 17%
-
-
?
linoleic acid + AH2 + O2
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
linolenic acid + AH2 + O2
arachidonic acid + A + H2O
linoleoyl phosphatidylcholine + AH2 + O2
gamma-linolenoylphosphatidylcholine + A + H2O
-
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
monogalactosydiacylglycerol + AH2 + O2
? + A + H2O
octadec-9,12-dienoic acid + AH2 + O2
octadec-6,9,12-trienoic acid + A + H2O
-
conversion rate is 11.5%
-
-
?
octadec-9-enoic acid + AH2 + O2
octadec-6,9-dienoic acid + A + H2O
-
conversion rate is 19.1%
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
octadecanoate + AH2 + O2
? + A + H2O
oleic acid + AH2 + O2
?
-
-
-
-
?
palmitate + AH2 + O2
sapienate + A + H2O
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
palmitoyl-[acyl-carrier protein] + reduced acceptor + O2
6-hexadecenoyl-[acyl-carrier protein] + acceptor + H2O
-
-
-
?
stearoyl-[acyl-carrier protein] + reduced acceptor + O2
6-octadecenoyl-[acyl-carrier protein] + 9-octadecenoyl-[acyl-carrier protein]acceptor + H2O
-
-
ratio of activity: 2/1
?
additional information
?
-
24-carbon fatty acid + AH2 + O2
? + A + H2O
-
-
-
-
?
24-carbon fatty acid + AH2 + O2
? + A + H2O
-
-
-
-
?
alpha-linolenic acid + AH2 + O2
?
preferred substrate
-
-
?
alpha-linolenic acid + AH2 + O2
?
-
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
conversion rate: 7.0
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
conversion rate: 31.5
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
-
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
-
conversion rate: 59.5
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
conversion rate: 23.1
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
conversion rate is 19%
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
conversion rates of 45.9%
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
conversion rates of 45.9%
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
?
alpha-linolenic acid + AH2 + O2
stearidonic acid + A + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
alpha-linoleoyl-CoA + AH2 + O2
stearidonoyl-CoA + A + 2 H2O
-
-
-
-
?
alpha-linoleoyl-CoA + AH2 + O2
stearidonoyl-CoA + A + 2 H2O
-
-
-
?
gamma-linolenic acid methyl ester + O2
?
-
7% conversion efficiency
-
-
?
gamma-linolenic acid methyl ester + O2
?
-
-
-
-
?
gamma-linolenic acid methyl ester + O2
?
-
-
-
-
?
linoleic acid + AH2 + O2
?
-
-
-
?
linoleic acid + AH2 + O2
?
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
conversion rate: 1.5
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
key enzyme localized in the endoplasmic reticulum
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
important for the generation of unsaturated fatty acids, DELTA6-desaturase required for the conversion of dietary linoleic acid to arachidonic acid
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
conversion rates of 14.2%
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
conversion rates of 14.2%
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
conversion rate: 3.6
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
important for the generation of unsaturated fatty acids, DELTA6-desaturase required for the conversion of dietary linoleic acid to arachidonic acid
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
14.4% conversion rate
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
conversion rate: 31.2
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
conversion rate: 12.2
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linolenic acid + AH2 + O2
arachidonic acid + A + H2O
-
-
-
?
linolenic acid + AH2 + O2
arachidonic acid + A + H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
preferred substrate
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
preferred substrate
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
-
-
-
-
?
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
-
-
-
?
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
-
-
-
-
?
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
monogalactosydiacylglycerol + AH2 + O2
? + A + H2O
-
-
-
-
?
monogalactosydiacylglycerol + AH2 + O2
? + A + H2O
-
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadeca-9,12-dienoic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
?
octadecanoate + AH2 + O2
? + A + H2O
-
-
-
-
?
octadecanoate + AH2 + O2
? + A + H2O
-
-
-
-
?
palmitate + AH2 + O2
sapienate + A + H2O
-
-
-
?
palmitate + AH2 + O2
sapienate + A + H2O
the enzyme is a component of the lipid metabolic pathway that converts the essential fatty acids linoleate and alpha-linolenate into long-chain polyunsaturated fatty acids. The DELTA-6 desaturase/FADS2 expressed in human sebocytes catalyzes the conversion of palmitate into sapienate
-
-
?
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
-
-
-
-
?
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
-
key enzyme required for numerous vital functions involving distinct polyunsaturated fatty acids and polyunsaturated fatty acid-derived bioactive lipids. It seems that the biological importance of DELTA6-desaturase activity should also be considered for its newly identified role in the control of the biosynthesis of a monoenoic fatty acid (C16:1 n-10), particularly in tissues with low DELTA9-desaturase activity
-
-
?
additional information
?
-
-
low activity with C15:1DELTA9 fatty acid and C16:1DELTA9 fatty acid
-
-
?
additional information
?
-
the zebrafish enzyme is a bifunctional DELTA5/DELTA6 desaturase
-
-
?
additional information
?
-
-
the enzyme is essential for the formation of long-chain metabolites from dietary linoleic acid and alpha-linolenic acid, but shows a slow activity in humans. A defect in the activity of DELTA6 and DELTA5 desaturases decreases the formation of gamma-linolenic acid, dihomo-gamma-linoleic acid, arachidonic acid, eicosapentaenoic acid, and docosahexaenoic acid from dietary linoleic acid, and alpha-linolenic acid. This, in turn, leads to inadequate formation of prostaglandins E1 and I3, prostacyclin, lipoxins resolvins, neuroprotectin D1, NO, and nitrolipids that have anti-inflammatory and platelet anti-aggregatory actions, inhibit leukocyte activation, augment wound healing, and resolve inflammation and thus, leads to the initiation and progression of atheroslcerosis, metabolism of essential fatty acids, overview, enzyme activity is decreased in diabetes mellitus, hypertension, hyperlipidemia, and metabolic syndrome X
-
-
?
additional information
?
-
-
alpha-linoleic acid is converted to eicosapentaenoic acid by the enzyme, the enzyme is also active with linoleic, which is converted to gamma-linoleic acid, and oleic acid
-
-
?
additional information
?
-
-
D6D activity in preterm, term, and post-natals is estimated by the 20:3n-6/18:2n-6 ratio
-
-
?
additional information
?
-
-
PiDes6 desaturates both omegax6 and omega3 substrates, substrate specificity in comparison to other fatty acid desaturases, overview
-
-
?
additional information
?
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
-
-
?
additional information
?
-
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
-
-
?
additional information
?
-
the enzyme MpFADS6 shows a substrate preference for alpha-linolenoyl-CoA, sequences between the histidine boxes I and II plays a pivotal role in substrate preference, mutational analysis, substrate specificities of wild-type and mutant enzymes, overview. MpFADS6 has a preference for the alpha-linolenoyl-CoA substrate with a 66.5% conversion rate
-
-
?
additional information
?
-
-
the enzyme MpFADS6 shows a substrate preference for alpha-linolenoyl-CoA, sequences between the histidine boxes I and II plays a pivotal role in substrate preference, mutational analysis, substrate specificities of wild-type and mutant enzymes, overview. MpFADS6 has a preference for the alpha-linolenoyl-CoA substrate with a 66.5% conversion rate
-
-
?
additional information
?
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
-
-
?
additional information
?
-
the enzyme MpFADS6 shows a substrate preference for alpha-linolenoyl-CoA, sequences between the histidine boxes I and II plays a pivotal role in substrate preference, mutational analysis, substrate specificities of wild-type and mutant enzymes, overview. MpFADS6 has a preference for the alpha-linolenoyl-CoA substrate with a 66.5% conversion rate
-
-
?
additional information
?
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
-
-
?
additional information
?
-
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
-
-
?
additional information
?
-
polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
-
-
?
additional information
?
-
-
polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
-
-
?
additional information
?
-
the enzyme MaFADS6-I shows a substrate preference for linoleoyl-CoA, sequences between the histidine boxes I and II plays a pivotal role in substrate preference, mutational analysis, substrate specificities of wild-type and mutant enzymes, overview. When a single substrate is added, linoleoyl-CoA and alpha-linolenoyl-CoA are catalyzed by MaFADS6 with conversion rates of 45.6% and 19.6%, respectively. When linoleoyl-CoA and alpha-linolenoyl-CoA are added at the same time, the linoleoyl-CoA conversion rate reaches 58.4%, but alpha-linolenoyl-CoA conversion decreases to 2.0%
-
-
?
additional information
?
-
-
the enzyme MaFADS6-I shows a substrate preference for linoleoyl-CoA, sequences between the histidine boxes I and II plays a pivotal role in substrate preference, mutational analysis, substrate specificities of wild-type and mutant enzymes, overview. When a single substrate is added, linoleoyl-CoA and alpha-linolenoyl-CoA are catalyzed by MaFADS6 with conversion rates of 45.6% and 19.6%, respectively. When linoleoyl-CoA and alpha-linolenoyl-CoA are added at the same time, the linoleoyl-CoA conversion rate reaches 58.4%, but alpha-linolenoyl-CoA conversion decreases to 2.0%
-
-
?
additional information
?
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
-
-
?
additional information
?
-
the enzyme MaFADS6-I shows a substrate preference for linoleoyl-CoA, sequences between the histidine boxes I and II plays a pivotal role in substrate preference, mutational analysis, substrate specificities of wild-type and mutant enzymes, overview. When a single substrate is added, linoleoyl-CoA and alpha-linolenoyl-CoA are catalyzed by MaFADS6 with conversion rates of 45.6% and 19.6%, respectively. When linoleoyl-CoA and alpha-linolenoyl-CoA are added at the same time, the linoleoyl-CoA conversion rate reaches 58.4%, but alpha-linolenoyl-CoA conversion decreases to 2.0%
-
-
?
additional information
?
-
polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
-
-
?
additional information
?
-
-
polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
-
-
?
additional information
?
-
the FADS2 product introduces a double bond at the DELTA6, DELTA4 and DELTA8 positions by acting on at least ten substrates, including fatty acids 16:0, 18:2n-6, and 18:3n-3. MCF7 cells stably transformed with FADS2 biosynthesizes fatty acid 16:1n-10 from exogenous fatty acid 16:0, fatty acid 18:4n-3 from fatty acid 18:3n-3, fatty acid 18:3n-6 from fatty acid 18:2n-6, fatty acid 18:2n-9 from fatty acid 18:1n-9, fatty acid 24:6n-3 from fatty acid 24:5n-3 and fatty acid 24:5n-6 from fatty acid 24:4n-6
-
-
?
additional information
?
-
fatty acid DELTA6-desaturation is the first commited step in C20 polyunsaturated fatty acid biosynthesis
-
-
?
additional information
?
-
fatty acid DELTA6-desaturation is the first commited step in C20 polyunsaturated fatty acid biosynthesis
-
-
?
additional information
?
-
no activity with linoleic acid
-
-
?
additional information
?
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with by DELTA6fad_b
-
-
?
additional information
?
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with by DELTA6fad_b
-
-
?
additional information
?
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with by DELTA6fad_b
-
-
?
additional information
?
-
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with by DELTA6fad_b
-
-
?
additional information
?
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with DELTA6fad_c
-
-
?
additional information
?
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with DELTA6fad_c
-
-
?
additional information
?
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with DELTA6fad_c
-
-
?
additional information
?
-
-
no activity with 20:4n-3, 20:3n-6, 22:5n-3, and 22:4n-6 with DELTA6fad_c
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
alpha-linoleoyl-CoA + AH2 + O2
stearidonoyl-CoA + A + 2 H2O
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
linoleoyl-CoA + AH2 + O2
gamma-linolenoyl-CoA + A + 2 H2O
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
palmitate + AH2 + O2
sapienate + A + H2O
the enzyme is a component of the lipid metabolic pathway that converts the essential fatty acids linoleate and alpha-linolenate into long-chain polyunsaturated fatty acids. The DELTA-6 desaturase/FADS2 expressed in human sebocytes catalyzes the conversion of palmitate into sapienate
-
-
?
palmitic acid + AH2 + O2
hexadec-6-enoic acid + A + H2O
-
key enzyme required for numerous vital functions involving distinct polyunsaturated fatty acids and polyunsaturated fatty acid-derived bioactive lipids. It seems that the biological importance of DELTA6-desaturase activity should also be considered for its newly identified role in the control of the biosynthesis of a monoenoic fatty acid (C16:1 n-10), particularly in tissues with low DELTA9-desaturase activity
-
-
?
additional information
?
-
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
-
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenic acid + AH2 + O2
octadec-6,9,12,15-tetraenoic acid + A + 2 H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
?
alpha-linolenoyl-CoA + ferrocytochrome b5 + O2 + H+
stearidonoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
key enzyme localized in the endoplasmic reticulum
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
important for the generation of unsaturated fatty acids, DELTA6-desaturase required for the conversion of dietary linoleic acid to arachidonic acid
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
important for the generation of unsaturated fatty acids, DELTA6-desaturase required for the conversion of dietary linoleic acid to arachidonic acid
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
DELTA6-desaturase reaction is the rate-limiting step in the conversion of linoleic acid and alpha linoleic acids to the longer, more highly unsaturated members of the n-6 and n-3 polyunsaturated fatty acids, metabolic pathway in mammalian cells
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
the enzyme is responsible for the first and rate-limiting step in biosynthesis of highly unsaturated fatty acids
-
-
?
linoleic acid + AH2 + O2
gamma-linolenic acid + A + H2O
-
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
preferred substrate
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
linoleoyl-CoA + ferrocytochrome b5 + O2 + H+
gamma-linolenoyl-CoA + ferricytochrome b5 + H2O
-
-
-
-
?
additional information
?
-
the zebrafish enzyme is a bifunctional DELTA5/DELTA6 desaturase
-
-
?
additional information
?
-
-
the enzyme is essential for the formation of long-chain metabolites from dietary linoleic acid and alpha-linolenic acid, but shows a slow activity in humans. A defect in the activity of DELTA6 and DELTA5 desaturases decreases the formation of gamma-linolenic acid, dihomo-gamma-linoleic acid, arachidonic acid, eicosapentaenoic acid, and docosahexaenoic acid from dietary linoleic acid, and alpha-linolenic acid. This, in turn, leads to inadequate formation of prostaglandins E1 and I3, prostacyclin, lipoxins resolvins, neuroprotectin D1, NO, and nitrolipids that have anti-inflammatory and platelet anti-aggregatory actions, inhibit leukocyte activation, augment wound healing, and resolve inflammation and thus, leads to the initiation and progression of atheroslcerosis, metabolism of essential fatty acids, overview, enzyme activity is decreased in diabetes mellitus, hypertension, hyperlipidemia, and metabolic syndrome X
-
-
?
additional information
?
-
-
D6D activity in preterm, term, and post-natals is estimated by the 20:3n-6/18:2n-6 ratio
-
-
?
additional information
?
-
-
PiDes6 desaturates both omegax6 and omega3 substrates, substrate specificity in comparison to other fatty acid desaturases, overview
-
-
?
additional information
?
-
delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
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additional information
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delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
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additional information
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delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
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additional information
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delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
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additional information
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delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
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additional information
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polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
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additional information
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polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
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additional information
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delta 6 desaturase (FADS6) is a key bifunctional enzyme desaturating linoleic acid or alpha-linolenic acid, analysis of the molecular mechanism of substrate specificity, overview
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?
additional information
?
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polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
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additional information
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polyunsaturated fatty acid profiles in Mortierella alpina, the lipids are synthesized mainly via the omega6 pathway and rarely via the omega3 pathway and as a result contain low alpha-linolenoyl-CoA and eicosapentaenoic acid levels
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additional information
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fatty acid DELTA6-desaturation is the first commited step in C20 polyunsaturated fatty acid biosynthesis
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additional information
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fatty acid DELTA6-desaturation is the first commited step in C20 polyunsaturated fatty acid biosynthesis
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evolution
phylogenetic tree of AsD6DES and delta 6- and delta 5-desaturases
evolution
weak activity and different secondary structure of delta-6 desaturase (D6DES) in Echium amoenum compared with D6DESs of other species
metabolism
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the enzyme takes part in the fatty Acid synthesis pathway, detailed overview
metabolism
delta 6-desaturase involved in very-long-chain polyunsaturated fatty acid synthesis
metabolism
fatty acid delta 6-desaturase (D6DES) and elongases are key enzymes in the synthesis of polyunsaturated fatty acids (PUFAs) including arachidonic acid (ARA) and eicosapentaenoic acid (EPA) from microorganisms to higher animals. Proposed pathways of polyunsaturated fatty acid biosynthesis from a-linolenic acid and linoleic acid in Acanthopagrus schlegelii, overview
metabolism
the enzyme follows the omega3 and omega6 pathways. Regulation of surface-membrane enzymes such as delta-6-desaturase and secretory phospholipase A2 by hemp seed and evening primrose oils as well as hot-natured dietary intervention in relapsing remitting multiple sclerosis (RRMS) patients having beneficial effects in improving clinical symptoms and signs in the patients, possible mechanisms, overview
metabolism
the enzyme is involved in the aerobic very long chain-polyunsaturated fatty acid biosynthetic pathways, overview
metabolism
the enzyme is involved in the aerobic very long chain-polyunsaturated fatty acid biosynthetic pathways, overview
metabolism
the enzyme seems to be a rate-limiting enzyme of the long-chain polyunsaturated fatty acids (LC-PUFAs) biosynthesis
metabolism
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the enzyme is involved in the aerobic very long chain-polyunsaturated fatty acid biosynthetic pathways, overview
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metabolism
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delta 6-desaturase involved in very-long-chain polyunsaturated fatty acid synthesis
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metabolism
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the enzyme is involved in the aerobic very long chain-polyunsaturated fatty acid biosynthetic pathways, overview
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physiological function
fatty acid DELTA6-desaturase is the essential enzyme for polyunsaturated fatty acids biosynthesis and is responsible for the first step by converting linoleic acid to gamma-linolenoyl-CoA, and alpha-linolenic acid to stearidonic acid
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
mechanisms involved in the nutritional modulation of DELTA6D, overview
physiological function
D6DES enzyme is responsible for converting linoleic acid and alpha-linolenic acid to gamma-linolenoic acid and stearidonic acid
physiological function
delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for polyunsaturated fatty acid biosynthesis, high catalytic activity of FADS2s from Glossomastix chrysoplasta. It controls the conversion of linoleoyl-CoA and alpha-linolenoyl-CoA to gamma-linolenic acid and stearidonic acid, respectively
physiological function
delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for polyunsaturated fatty acid biosynthesis, high catalytic activity of FADS2s from Thalassiosira pseudonana. It controls the conversion of linoleoyl-CoA and alpha-linolenoyl-CoA to gamma-linolenic acid and stearidonic acid, respectively
physiological function
microbial species have different propensity for accumulating omega6- or omega3-series polyunsaturated fatty acids, which may be determined by the substrate preference of FADS6 enzyme, molecular mechanism of FADS6 substrate specificity, overview. Micromonas pusilla strain CCMP1545 synthesizes high levels of eicosapentaenoic acid
physiological function
microbial species have different propensity for accumulating omega6- or omega3-series polyunsaturated fatty acids, which may be determined by the substrate preference of FADS6 enzyme, molecular mechanism of FADS6 substrate specificity, overview. Mortierella alpina strain ATCC 32222 synthesizes high levels of arachidonic acid
physiological function
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neonates have high delta-6 desaturase (D6D) activity, which is important for regulating polyunsaturated fatty acid's (PUFA) nutritional status. At birth, preterm infants have D6D activity as high as that of term infants, D6D activity declines to about one-third at one month, then further decreases to about one-sixth at six months and remained stable until 12 months. The postnatal change in arachidonic acid exhibits a similar pattern to that of D6D activity. Docosahexaenoic acid shows a transient decrease at one month and recovers to the cord blood level at six months. Enzyme D6D may regulate PUFA profile in preterm infants, especially during the early postnatal period. Long-chain polyunsaturated fatty acids (PUFAs), such as arachidonic acid (AA) and docosahexaenoic acid (DHA), are critical nutrients for humans, as humans do not have the enzymes to synthesize PUFA from acetyl CoA, but are instead able to produce AA and DHA from precursor PUFAs, linoleic acid (LA), and alpha-linolenic acid (ALA), respectively
physiological function
regulation of surface-membrane enzymes such as delta-6-desaturase and secretory phospholipase A2 by hemp seed and evening primrose oils as well as hot-natured dietary intervention in relapsing remitting multiple sclerosis (RRMS) patients having beneficial effects in improving clinical symptoms and signs in the patients, possible mechanisms, overview. FADS2 enzyme catalyzes the rate-limiting step in the biosynthetic pathways for polyunsaturated fatty acids that are incorporated into cell membranes, thereby affecting permeability, and functional propertiesof cells. There isa correlation between multile sclerosis and a rapid fall of FADS6 enzyme activity
physiological function
the FADS2 genotype regulates delta-6 desaturase activity and inflammation in human adipose tissue, association between fatty acid metabolism and adipose tissue inflammation in the Kuopio obesity surgery study, altered interleukin-1beta and NF-kappaB pathway gene expressio, overview. D6D enzyme activity in serum triglyceride fraction correlates with interleukin-1beta expression in subcutaneous adipose tissue. Surgery-induced weight loss is correlated with genotype FADS2
physiological function
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microbial species have different propensity for accumulating omega6- or omega3-series polyunsaturated fatty acids, which may be determined by the substrate preference of FADS6 enzyme, molecular mechanism of FADS6 substrate specificity, overview. Mortierella alpina strain ATCC 32222 synthesizes high levels of arachidonic acid
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physiological function
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microbial species have different propensity for accumulating omega6- or omega3-series polyunsaturated fatty acids, which may be determined by the substrate preference of FADS6 enzyme, molecular mechanism of FADS6 substrate specificity, overview. Micromonas pusilla strain CCMP1545 synthesizes high levels of eicosapentaenoic acid
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additional information
comparison of seawater and freshwater fish desaturated fatty acid comtents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid comtents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
comparison of seawater and freshwater fish desaturated fatty acid contents, expression profiles and substrate specificities, overview
additional information
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fat-3 mutant phenotype, lifespan, and transgenerational effect of cis- and trans-triglyceride diets, overview
additional information
nutritional regulation, overview
additional information
nutritional regulation, overview
additional information
nutritional regulation, overview
additional information
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nutritional regulation, overview
additional information
analysis of functional sites and substrate binding motifs of D6DES enzyme, overview
additional information
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polyunsaturated fatty acid profile at birth and its postnatal change, overview
additional information
structure-function relationship, domain-swapping approach, two regions are essential to the catalytic mechanism: one that extends from the end of the fourth to the beginning of the fifth cytoplasmic transmembrane domain, and another that includes the C-terminal region that occurs after the sixth cytoplasmic transmembrane domain. Fatty acid contents of wild-type an dmutant strains, overview
additional information
structure-function relationship, domain-swapping approach, two regions are essential to the catalytic mechanism: one that extends from the end of the fourth to the beginning of the fifth cytoplasmic transmembrane domain, and another that includes the C-terminal region that occurs after the sixth cytoplasmic transmembrane domain. Fatty acid contents of wild-type and mutant strains, overview
additional information
the enzyme sequence displays the typical structure of microsomal FADS2 including two transmembrane domains and an N-terminal cytochrome b5 domain with the HPGG motif
additional information
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the enzyme sequence displays the typical structure of microsomal FADS2 including two transmembrane domains and an N-terminal cytochrome b5 domain with the HPGG motif
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H129G
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
H129R
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
H305G
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
H305R
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
H89G
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity, can be rescued by 150 mM exogenous imidazole
H89R
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity using linoleic acid as substrate
H129G
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
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H129R
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity using linoleic acid as substrate
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H305G
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, no enzyme activity, can be rescued by 150 mM exogenous imidazole
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H89G
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity, can be rescued by 150 mM exogenous imidazole
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H89R
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expressed in Saccharomyces cerevisiae, grown in SD medium in the presence of 50 microM of linoleic acid substrate, very low enzyme activity using linoleic acid as substrate
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D313I
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
D367H
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
F310L
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
I390L
site-directed mutagenesis, mutant shows similar activity with linoleoyl-CoA and reduced activity with alpha-linolenoyl-CoA compared to the wild-type enzyme
M384S/M385L
site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme
N388H
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
S306T
site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme
S322A
site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme
Y375F
site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme
E222S
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
G194L
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is significantly reduced to 6.50% compared to the wild-type enzyme
M227K
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
Q209G
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
S197Q
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
V189L/Q190A
site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
V399I/I400E
site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
G194L
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site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is significantly reduced to 6.50% compared to the wild-type enzyme
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M227K
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site-directed mutagenesis, the mutant's relative conversion rate of alpha-linolenoyl-CoA is reduced by almost 50% compared to the wild-type enzyme
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S197Q
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site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
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V189L/Q190A
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site-directed mutagenesis, the mutation does not lead to major changes in substrate preference
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G390D
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amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain YB214
T375K
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amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain HR95
W314Stop
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amino acid replacement in isoenzyme DELTA6I of DELTA6 desaturase-defective mutant strain ST66
A361Q
activity is significantly lower than that of wild-type enzyme
F166V/V167L
activity is significantly lower than that of wild-type enzyme
F356V/S358T
activity is significantly lower than that of wild-type enzyme
H410Y/E413K
activity is significantly lower than that of wild-type enzyme
I192T
activity is significantly lower than that of wild-type enzyme
K234N/S235M/L236delta
decreased or null DELTA6 desaturase activity
K234N/S235M/L236DELTA/K444Q
activity is significantly lower than that of wild-type enzyme
K444Q
decreased or null DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/V344P
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/I326V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/F370A/Y352N/I326V/Y188F/K190T/H410Y/E413K
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/I195L/W245V/L396Y/Y257H/V344P/I284F/Y352N/I326V/H410Y
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
N156T/A305V/Y182F/K234N/S235M/E365K/F166V/L423F/L424A/L248V/F322L/L323F/W245V
acquisition of DELTA5 desaturase activity without losing DELTA6 desaturase activity
P246S/L247V/Y249L
activity is significantly lower than that of wild-type enzyme
Y352N/R353V
activity is significantly lower than that of wild-type enzyme
H360D
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
H381N
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
I306L
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
L303F
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
L383I
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
M384S/M385
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
S322A
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
T299S
site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme
T302V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y375F
site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme
A181T/A188G/Y189F/S205N/L206T/G207A
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compared to wild-type: reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, strong DELTA9 desaturase activity with stearoyl-[acyl-carrier protein] as substrate, exhibits DELTA9 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate
A181T/A200F
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increase in DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, strong DELTA9 desaturase activity with stearoyl-[acyl-carrier protein] as substrate
A181T/A200F/S205N/L206T/G207A
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reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate, very low DELTA9 desaturase activity, no DELTA6 desaturase activity with stearoyl-[acyl-carrier protein] as substrate
A188G/Y189F
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reduced DELTA6 desaturase activity with palmitoyl-[acyl-carrier protein] as substrate
T302V
site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme
T302V
site-directed mutagenesis, mutant shows potently increased activity compared to the wild-type enzyme
DELTA238P/DELTA239L
activity is significantly lower than that of wild-type enzyme
DELTA238P/DELTA239L
decreased or null DELTA6 desaturase activity
Q415E/E416S
activity is significantly lower than that of wild-type enzyme
Q415E/E416S
decreased or null DELTA6 desaturase activity
R216M
activity is significantly lower than that of wild-type enzyme
R216M
decreased or null DELTA6 desaturase activity
S209P/N211S
activity is significantly lower than that of wild-type enzyme
S209P/N211S
decreased or null DELTA6 desaturase activity
additional information
construction of chimeric enzymes of delta6 desaturases from Glossomastix chrysoplasta and Thalassiosira pseudonana, chimera 7 with GcFADS2 residues 285-315 replaced by TpFADS2 residues 291-324 shows about 5fold increased activity with both substrates compared to the wild-type enzyme, the catalytic efficiency of chimera 9 with GcFADS2 residues 359-458 replaced by TpFADS2 residues 370-484 is also increased. The other chimeras exhibit a catalytic efficiency not significantly different both substrates compared with that exhibited by wild-type GcFADS2/TpFADS2. Fatty acid contents of wild-type and mutant strains, overview
additional information
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genetic polymorphism of DELTA6 desaturase are naturally occuring in humans, a delivery of the gene for D6 desaturase to endothelial cells at atherosclerosis prone areas is expected to prevent/arrest the development of atherosclerosis despite the presence of hyperlipidemia, hypertension, diabetes mellitus, and at sites of shear stress of blood flow
additional information
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the former from Mortierella alpina strain ATCC 32222, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
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construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the former from Mortierella alpina strain ATCC 32222, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
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construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the former from Mortierella alpina strain ATCC 32222, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
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additional information
construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the latter from Micromonas pusilla strain CCMP1545, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
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construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the latter from Micromonas pusilla strain CCMP1545, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
additional information
recombinant overexpression of Micromonas pusilla strain CCMP 1545 enzyme MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina, fatty acid profile with addition of exogenous alpha-linolenoic acid. Further enhancement of EPA production with peony seed meal, overview
additional information
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recombinant overexpression of Micromonas pusilla strain CCMP 1545 enzyme MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina, fatty acid profile with addition of exogenous alpha-linolenoic acid. Further enhancement of EPA production with peony seed meal, overview
additional information
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construction of chimeric mutant genes from MaFADS6 and MpFADS6 genes, the latter from Micromonas pusilla strain CCMP1545, overview. The relative conversion rate for linoleoyl-CoA remains low in all mutants compared to the wild-type enzyme
-
additional information
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recombinant overexpression of Micromonas pusilla strain CCMP 1545 enzyme MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina, fatty acid profile with addition of exogenous alpha-linolenoic acid. Further enhancement of EPA production with peony seed meal, overview
-
additional information
generation of a series deletion analysis of the promoter suggesting that the sequence between -919 to -784 bp (relative to start site), termed eMd6, is the key factor for high activity of DELTA6-desaturase. Deletion of sequence between -919 and -784 bp (pYD6784-Md6), that contains three TATA boxes, a CREB1 site, and a potential promoter region, significantly reduces DELTA6-desaturase activity to 77% that of pYD6919-Md6. Further deletion of sequence from -644 to -434 bp (pYD6434-Md6), -434 to -121 (pYD6121-Md6) significantly reduces Md6 promoter activity to less than 40 and 13% that of the predecessor
additional information
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generation of a series deletion analysis of the promoter suggesting that the sequence between -919 to -784 bp (relative to start site), termed eMd6, is the key factor for high activity of DELTA6-desaturase. Deletion of sequence between -919 and -784 bp (pYD6784-Md6), that contains three TATA boxes, a CREB1 site, and a potential promoter region, significantly reduces DELTA6-desaturase activity to 77% that of pYD6919-Md6. Further deletion of sequence from -644 to -434 bp (pYD6434-Md6), -434 to -121 (pYD6121-Md6) significantly reduces Md6 promoter activity to less than 40 and 13% that of the predecessor
-
additional information
construction of chimeric enzymes of delta6 desaturases from Glossomastix chrysoplasta and Thalassiosira pseudonana, e.g. chimera 16 with TpFADS2 residues 291-324 replaced by GcFADS2 residues 285-315 shows decreased activity with both substrates compared to the wild-type enzyme. The replacement of the aa359-458 region of GcFADS2 results in a significant reduction in catalytic activity against both substrates, such that chimera 18 exhibits a decreased catalytic efficiency which represents the lowest rate observed among the TpFADS2 chimeras. The other chimeras exhibit a catalytic efficiency not significantly different both substrates compared with that exhibited by wild-type GcFADS2/TpFADS2. Fatty acid contents of wild-type an dmutant strains, overview
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D6D, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
D6D-V, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
DELTA6-desaturase gene identified in human chromosome 11
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DELTA6-desaturase II cDNA expressed in Aspergillus oryzae
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression in Saccharomyces cerevisiae strain INVSc1
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expressed in Camelina sativa
expressed in Escherichia coli DH5alpha, co-expressed with cytochrome b5 and ferredoxin, no enzyme activity when expressed in Escherichia coli alone
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expressed in HEK-293 cells
expressed in Pichia pastoris GS115
expressed in Pichia pastoris strain GS115
expressed in Saccharomyces cerevisiae
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expressed in Saccharomyces cerevisiae strain BY4741, two different mRNA variants
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expressed in Saccharomyces cerevisiae strain InvSc1
expressed in Saccharomyces cerevisiae strain INVScl
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expressed in Saccharomyces cerevisiae, strain DBY746 with and without supplementation with linoleic acid
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expression in Saccharomyces cerevisaiae
expression in Saccharomyces cerevisiae
expression of N-terminal truncated enzyme in Escherichia coli
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expression of wild-type, A181T/A188G/Y189F/S205N/L206T/G207A, A188G/Y189F, A181T/A200F and A181T/A200F/S205N/L206T/G207A mutant enzyme in Escherichia coli
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gene D6, recombinant expression in Saccharomyces
gene d6-des, DNA and amino acid sequence determination and analysis, sequence comparisons
gene D6DES, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, functional expression in Saccharomyces cerevisiae strain INVSc1 producing gamma-linolenic acid and stearidonic acid at conversion rates of 26.3-35.6% from exogenous linoleic acid and alpha-linolenic acid substrates, respectively. Fatty acid profiles of GC analysis from transgenic Saccharomyces cerevisiae strain INVSc1, overview
gene DELTA6fad_a, several variants, genetic structure, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae
gene DELTA6fad_b, several variants, genetic structure, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae
gene DELTA6fad_c, several variants, genetic structure, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Saccharomyces cerevisiae
gene desD, functional analysis of the Spirulina promoter in Escherichia coli, the -10 sequence, TATAAT, located at -33 bp relative to the translation start site, is essential for D6D promoter function, an AT-rich inverted repeat -192 to -164 serves as a target-binding site for a transcriptional regulator
gene desI, recombinant expression in Saccharomyces
gene fads2, DNA and amino acid sequence determination and analysis, cloning of two alternative splicing transcripts named fads2-AS1 and fads2-AS2, quantitative real-time PCR expression analysis, recombinant expression in yeast, which shows fully functional DELTA6 desaturation activity toward C18 polyunsaturated fatty acid substrates, without residual DELTA5 and DELTA8 desaturase activities
gene FADS2, rs174616 genotype, genotyping
gene FADS6, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain INVSc1, subcloning in Escherichia coli Top 10 cells
gene fadsd6, real-time PCR enzyme expression and copy number analysis, recombinant expression in Danio rerio. The eicosapentaenoic acid (EPA) content is 1.9fold higher in F2 transgenic delta-6 desaturase transgenic zebrafish than in wild-type fish, the fish exhibiting FADS6 enzyme expression are bigger than wild-type fish. henotype, overview. By 48 h post-infection with Vibrio alginolyticus, expression of IL-10 gene is 3.3fold higher in delta-6 desaturase transgenic fish than in wild-type fish. Expression of TLR1, TLR3, TLR4, TRAM, and NF-kappaB is also significantly different between the transgenic and wild-type fish
gene fat-3, quantitative real-time PCR expression analysis, overview
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gene Md6, DNA and amino acid sequence determination and analysis, Md6 promoter analysis in the 5'-upstream sequence, gene Md6 contains several eukaryotic fundamental transcription regulatory elements, sequence comparisons, functional recombinant expression in Saccharomyces cerevisiae strain INVSc1, the enzyme expression renders the yeast cells capable of converting linolenic acid to gamma-linolenic acid. The activity of DELTA6-desaturase increases by 2.8fold and 2.5fold when the mutant eMd6 sequence is placed upstream of -434 with forward or reverse orientations, respectively. The wild-type promoter of Md6 from Mucor sp. is a very strong promoter for DELTA6-desaturase and the sequence between -919 to -784 bp is an enhancer for DELTA6-desaturase activity
gene ObD6Des, DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression in Saccharomyces cerevisiae strain W303-a
gene PiDesD6, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression in Saccharomyces cerevisiae strain W303, real-time quantitative PCR expression analysis
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human sequence determined
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phylogenetic tree, expression in Pichia pastoris GS115, molecular mechanisms underlying the elevated expression of fatty acid desaturases induced by a decrease in the environmental temperature
plasmid coding for rat delta6-desaturase constructed using pCMV for expression in mammalian cells, rat delta6-desaturase sequence, GenBank accession number AB02 1980 PCR amplified, expressed by transiently transforming COS-7 cells
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recombinant overexpression of MpFADS6 in a uracil-auxotrophic Mortierella alpina strain to enhance eicosapentaenoic acid production in Mortierella alpina by favoring the omega3 pathway, using the Agrobacterium tumefaciens-mediated transformation method. The expression of MpFADS6 results in a 26.2fold increase in EPA production compared to wild-type Mortierella alpina
RT-PCR analysis of INS-1 beta-cell content of mRNA, primer pairs basedon known rat sequence
-
Saccharomyces cerevisiae transformed with fungal DELTA6-desaturase gene
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transformed into Agrobacterium tumefaciens and expressed in Glycine max
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expressed in Camelina sativa
-
expressed in Camelina sativa
-
expressed in Camelina sativa
-
expressed in Saccharomyces cerevisiae strain InvSc1
-
expressed in Saccharomyces cerevisiae strain InvSc1
-
expressed in Saccharomyces cerevisiae strain InvSc1
-
expressed in Saccharomyces cerevisiae strain InvSc1
expressed in Saccharomyces cerevisiae strain InvSc1
-
expressed in Saccharomyces cerevisiae strain InvSc1
expression in Saccharomyces cerevisaiae
-
expression in Saccharomyces cerevisaiae
expression in Saccharomyces cerevisaiae
expression in Saccharomyces cerevisaiae
expression in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae
gene FADS6, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain INVSc1, subcloning in Escherichia coli Top 10 cells
gene FADS6, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain INVSc1, subcloning in Escherichia coli Top 10 cells
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Jeffcoat, R.; Dunton, A.P.; James, A.T.
Evidence for the different responses of delta9-, delta6- and delta5-fatty acyl-CoA desaturases to cytoplasmic proteins
Biochim. Biophys. Acta
528
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Rattus norvegicus
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Linum usitatissimum, Spinacia oleracea
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Rattus norvegicus
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Rattus norvegicus, Rattus norvegicus Wistar
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Rattus norvegicus, Rattus norvegicus Wistar
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Arabidopsis thaliana, Glycine max, Spinacia oleracea, Arabidopsis thaliana Heynh.
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Rodriguez, A.; Sarda, P.; Boulot, P.; Leger, C.L.; Descomps, B.
Differential effect of N-ethyl maleimide on delta6-desaturase activity in human fetal liver toward fatty acids of the n-6 and n-3 series
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1999
Homo sapiens, Rattus norvegicus
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Brown, J.E.; Lindsay, R.M.; Riemersma, R.A.
Linoleic acid metabolism in the spontaneously diabetic rat: delta6-desaturase activity vs. product/precursor ratios
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Homo sapiens, Rattus norvegicus
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Effect of conjugated linoleic acid on fungal DELTA6-desaturase activity in a transformed yeast system
Lipids
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2001
Mortierella alpina
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Williard, D.E.; Nwankwo, J.O.; Kaduce, T.L.; Harmon, S.D.; Irons, M.; Moser, H.W.; Raymond, G.V.; Spector, A.A.
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Homo sapiens, Mus musculus, Rattus norvegicus
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The same rat DELTA6-desaturase not only acts on 18- but also on 24-carbon fatty acids in very-long-chain polyunsaturated fatty acid biosynthesis
Biochem. J.
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2002
Homo sapiens, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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Ramanadham, S.; Zhang, S.; Ma, Z.; Wohltmann, M.; Bohrer, A.; Hsu, F.F.; Turk, J.
DELTA6-, stearoyl CoA-, and DELTA5-desaturase enzymes are expressed in beta-cells and are altered by increases in exogenous PUFA concentrations
Biochim. Biophys. Acta
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2002
Homo sapiens, Rattus norvegicus
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Cahoon, E.B.; Lindqvist, Y.; Schneider, G.; Shanklin, J.
Redesign of soluble fatty acid desaturases from plants from altered substrate specificity and double bond position
Proc. Natl. Acad. Sci. USA
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1997
Thunbergia alata
brenda
Cahoon, E.B.; Coughlan, S.J.; Shanklin, J.
Characterization of a structurally and functionally diverged acyl-acyl carrier protein desaturase from milkweed seed
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1997
Thunbergia alata
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Schultz, D.J.; Suh, M.C.; Ohlrogge, J.B.
Stearoyl-acyl carrier protein and unusual acyl-acyl carrier protein desaturase activities are differentially influenced by ferredoxin
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2000
Thunbergia alata
brenda
Domergue, F.; Abbadi, A.; Zahringer, U.; Moreau, H.; Heinz, E.
In vivo characterization of the first acyl-CoA DELTA6-desaturase from a member of the plant kingdom, the microalga Ostreococcus tauri
Biochem. J.
389
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2005
Ostreococcus tauri, Ostreococcus tauri (Q4JDG7)
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Guillou, H.; D'Andrea, S.; Rioux, V.; Jan, S.; Legrand, P.
The surprising diversity of DELTA6-desaturase substrates
Biochem. Soc. Trans.
32
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2004
Rattus norvegicus
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Saether, T.; Tran, T.N.; Rootwelt, H.; Christophersen, B.O.; Haugen, T.B.
Expression and regulation of DELTA5-desaturase, DELTA6-desaturase, stearoyl-coenzyme A (CoA) desaturase 1, and stearoyl-CoA desaturase 2 in rat testis
Biol. Reprod.
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2003
Rattus norvegicus
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Sakuradani, E.; Shimizu, S.
Gene cloning and functional analysis of a second DELTA6-fatty acid desaturase from an arachidonic acid-producing Mortierella fungus
Biosci. Biotechnol. Biochem.
67
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2003
Mortierella alpina (Q76LW8), Mortierella alpina
brenda
Abe, T.; Sakuradani, E.; Asano, T.; Kanamaru, H.; Ioka, Y.; Shimizu, S.
Identification of mutation sites on DELTA6 desaturase genes from Mortierella alpina 1S-4 mutants
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69
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2005
Mortierella alpina
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Zheng, X.; Seiliez, I.; Hastings, N.; Tocher, D.R.; Panserat, S.; Dickson, C.A.; Bergot, P.; Teale, A.J.
Characterization and comparison of fatty acyl DELTA6 desaturase cDNAs from freshwater and marine teleost fish species
Comp. Biochem. Physiol. B
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269-279
2004
Cyprinus carpio (Q9DEX6), Cyprinus carpio, Oncorhynchus mykiss (Q98SW7), Oncorhynchus mykiss, Scophthalmus maximus, Sparus aurata (Q8AY64)
brenda
Sayanova, O.V.; Beaudoin, F.; Michaelson, L.V.; Shewry, P.R.; Napier, J.A.
Identification of primula fatty acid DELTA6-desaturases with n-3 substrate preferences
FEBS Lett.
542
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2003
Primula vialii (Q84KG6), Primula farinosa (Q84KG8)
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FEBS Lett.
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Amylomyces rouxii
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Ge, L.; Gordon, J.S.; Hsuan, C.; Stenn, K.; Prouty, S.M.
Identification of the DELTA-6 desaturase of human sebaceous glands: expression and enzyme activity
J. Invest. Dermatol.
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2003
Homo sapiens (O95864), Homo sapiens
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Highly unsaturated fatty acid synthesis in vertebrates: new insights with the cloning and characterization of a DELTA6 desaturase of Atlantic salmon
Lipids
40
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2005
Salmo salar (Q6SES0), Salmo salar
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Jan, S.; Guillou, H.; D'Andrea, S.; Daval, S.; Bouriel, M.; Rioux, V.; Legrand, P.
Myristic acid increases DELTA6-desaturase activity in cultured rat hepatocytes
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Rattus norvegicus
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Wang, D.; Li, M.; Wei, D.; Cai, Y.; Zhang, Y.; Xing, L.
Identification and functional characterization of the DELTA 6-fatty acid desaturase gene from Thamnidium elegans
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Thamnidium elegans, Thamnidium elegans (Q58KB0), Thamnidium elegans As.3.2806, Thamnidium elegans As3.2806 (Q58KB0), Thamnidium elegans As3.2806
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Glossomastix chrysoplasta
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Kurdrid, P.; Subudhi, S.; Hongsthong, A.; Ruengjitchatchawalya, M.; Tanticharoen, M.
Functional expression of Spirulina-DELTA6 desaturase gene in yeast, Saccharomyces cerevisiae
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Arthrospira platensis, Arthrospira platensis C1
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Arthrospira platensis
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Co-expression of the borage DELTA6 desaturase and the Arabidopsis DELTA15 desaturase results in high accumulation of stearidonic acid in the seeds of transgenic soybean
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Borago officinalis
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Homo sapiens
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Siganus canaliculatus (B2KKL4), Siganus canaliculatus
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Rhizopus stolonifer (Q32VA4)
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Characterization and modulation of gene expression and enzymatic activity of DELTA-6 desaturase in teleosts: A review
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Monroig, O.; Zheng, X.; Morais, S.; Leaver, M.J.; Taggart, J.B.; Tocher, D.R.
Multiple genes for functional DELTA6 fatty acyl desaturases (Fad) in Atlantic salmon (Salmo salar L.): gene and cDNA characterization, functional expression, tissue distribution and nutritional regulation
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Salmo salar (D2KE02), Salmo salar (D2KE03), Salmo salar (Q6SES0), Salmo salar
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Acanthopagrus schlegelii
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Reisner, K.; Lehtonen, M.; Storvik, M.; Jantson, T.; Lakso, M.; Callaway, J.C.; Wong, G.
Trans fat diet causes decreased brood size and shortened lifespan in Caenorhabditis elegans DELTA-6-desaturase mutant fat-3
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Caenorhabditis elegans
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Identification and characterization of DELTA12, DELTA6, and DELTA5 desaturases from the green microalga Parietochloris incisa
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Lobosphaera incisa
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Santigosa, E.; Geay, F.; Tonon, T.; Le Delliou, H.; Kuhl, H.; Reinhardt, R.; Corcos, L.; Cahu, C.; Zambonino-Infante, J.L.; Mazurais, D.
Cloning, tissue expression analysis, and functional characterization of two DELTA6-desaturase variants of sea bass (Dicentrarchus labrax L.)
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Dicentrarchus labrax (B1PJR8), Dicentrarchus labrax (B2ZE91)
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Oenothera biennis (E1U2Q3)
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Lu, H.; Zhu, Y.
The thermostability of two kinds of recombinant DELTA6-fatty acid desaturase with different N-terminal sequence lengths in low temperature
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Chen, Q.; Nimal, J.; Li, W.; Liu, X.; Cao, W.
Delta-6 desaturase from borage converts linoleic acid to gamma-linolenic acid in HEK293 cells
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Borago officinalis (O04353), Borago officinalis
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Characterization of fatty acid delta-6 desaturase gene in Nile tilapia and heterogenous expression in Saccharomyces cerevisiae
Comp. Biochem. Physiol. B
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Oreochromis niloticus
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Cytochrome b5 coexpression increases Tetrahymena thermophila DELTA6 fatty acid desaturase activity in Saccharomyces cerevisiae
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Song, L.; Zhang, Y.; Li, S.; Hu, J.; Yin, W.; Chen, Y.; Hao, S.; Wang, B.; Wang, R.; Hu, Z.
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Planta
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Sayanova, O.; Ruiz-Lopez, N.; Haslam, R.P.; Napier, J.A.
The role of DELTA6-desaturase acyl-carrier specificity in the efficient synthesis of long-chain polyunsaturated fatty acids in transgenic plants
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10
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Mus musculus, Salmo salar, Ostreococcus tauri
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Echium amoenum (D2KP14)
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Park, H.G.; Kothapalli, K.S.D.; Park, W.J.; DeAllie, C.; Liu, L.; Liang, A.; Lawrence, P.; Brenna, J.T.
Palmitic acid (16 0) competes with omega-6 linoleic and omega-3 alpha-linolenic acids for FADS2 mediated DELTA6-desaturation
Biochim. Biophys. Acta
1861
91-97
2016
Papio anubis (B8R1K0)
brenda
Jiang, X.; Liu, H.; Niu, Y.; Qi, F.; Zhang, M.; Huang, J.
Functional identification and regulatory analysis of DELTA6-fatty acid desaturase from the oleaginous fungus Mucor sp. EIM-10
Biotechnol. Lett.
39
453-461
2017
Mucor sp. (B3GQC8), Mucor sp. EIM-10 (B3GQC8)
brenda
Kim, S.; Park, J.; Kim, S.; Kim, J.; Roh, K.; Kim, H.; Lee, K.; Kim, J.
Functional characterization of polyunsaturated fatty acid delta 6-desaturase and elongase genes from the black seabream (Acanthopagrus schlegelii)
Cell Biochem. Biophys.
68
335-346
2014
Acanthopagrus schlegelii (A0A1S5R926)
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brenda
Geay, F.; Tinti, E.; Mellery, J.; Michaux, C.; Larondelle, Y.; Perpete, E.; Kestemont, P.
Cloning and functional characterization of DELTA6 fatty acid desaturase (FADS2) in Eurasian perch (Perca fluviatilis)
Comp. Biochem. Physiol. B
191
112-125
2016
Perca fluviatilis (A0A0A1E9M5), Perca fluviatilis
brenda
Rezapour-Firouzi, S.; Arefhosseini, S.R.; Ebrahimi-Mamaghani, M.; Baradaran, B.; Sadeghihokmabad, E.; Mostafaei, S.; Torbati, M.; Chehreh, M.
Alteration of delta-6-desaturase (FADS2), secretory phospholipase-A2 (sPLA2) enzymes by Hot-nature diet with co-supplemented hemp seed, evening primrose oils intervention in multiple sclerosis patients
Complement. Ther. Med.
23
652-657
2015
Homo sapiens (O95864), Homo sapiens
brenda
Wang, Y.D.; Peng, K.C.; Wu, J.L.; Chen, J.Y.
Transgenic expression of salmon DELTA-5 and DELTA-6 desaturase in zebrafish muscle inhibits the growth of Vibrio alginolyticus and affects fish immunomodulatory activity
Fish Shellfish Immunol.
39
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2014
Salmo salar (Q6SES0)
brenda
Lopez-Vicario, C.; Gonzalez-Periz, A.; Rius, B.; Moran-Salvador, E.; Garcia-Alonso, V.; Lozano, J.; Bataller, R.; Cofan, M.; Kang, J.; Arroyo, V.; Claria, J.; Titos, E.
Molecular interplay between DELTA5/DELTA6 desaturases and long-chain fatty acids in the pathogenesis of non-alcoholic steatohepatitis
Gut
63
344-355
2014
Mus musculus (F2WWK6)
brenda
Yary, T.; Voutilainen, S.; Tuomainen, T.P.; Ruusunen, A.; Nurmi, T.; Virtanen, J.K.
Omega-6 polyunsaturated fatty acids, serum zinc, delta-5- and delta-6-desaturase activities and incident metabolic syndrome
J. Hum. Nutr. Diet.
30
506-514
2017
Homo sapiens (O95864), Homo sapiens
brenda
Shi, H.; Chen, H.; Gu, Z.; Song, Y.; Zhang, H.; Chen, W.; Chen, Y.Q.
Molecular mechanism of substrate specificity for delta 6 desaturase from Mortierella alpina and Micromonas pusilla
J. Lipid Res.
56
2309-2321
2015
Micromonas pusilla (A0A172SZR2), Micromonas pusilla, Mortierella alpina (Q70BL2), Mortierella alpina, Mortierella alpina ATCC 32222 (Q70BL2), Micromonas pusilla CCMP 1545 (A0A172SZR2)
brenda
Vaittinen, M.; Walle, P.; Kuosmanen, E.; Maennistoe, V.; Kaekelae, P.; Agren, J.; Schwab, U.; Pihlajamaeki, J.
FADS2 genotype regulates delta-6 desaturase activity and inflammation in human adipose tissue
J. Lipid Res.
57
56-65
2016
Homo sapiens (O95864), Homo sapiens
brenda
Watanabe, K.; Ohno, M.; Taguchi, M.; Kawamoto, S.; Ono, K.; Aki, T.
Identification of amino acid residues that determine the substrate specificity of mammalian membrane-bound front-end fatty acid desaturases
J. Lipid Res.
57
89-99
2016
Rattus norvegicus (Q9Z122)
brenda
Shi, H.; Wu, R.; Zheng, Y.; Yue, X.
Molecular mechanisms underlying catalytic activity of delta 6 desaturase from Glossomastix chrysoplasta and Thalassiosira pseudonana
J. Lipid Res.
59
79-88
2017
Glossomastix chrysoplasta (Q49S39), Thalassiosira pseudonana (Q4G2T1)
brenda
Shi, H.; Chen, H.; Gu, Z.; Zhang, H.; Chen, W.; Chen, Y.Q.
Application of a delta-6 desaturase with alpha-linolenic acid preference on eicosapentaenoic acid production in Mortierella alpina
Microb. Cell Fact.
15
117
2016
Micromonas pusilla (C1MKR5), Micromonas pusilla, Mortierella alpina (Q70BL2), Mortierella alpina, Mortierella alpina ATCC 32222 (Q70BL2), Mortierella alpina ATCC 32222, Micromonas pusilla CCMP 1545 (C1MKR5)
brenda
Nagano, N.; Okada, T.; Kayama, K.; Hosono, S.; Kitamura, Y.; Takahashi, S.
Delta-6 desaturase activity during the first year of life in preterm infants
Prostaglandins Leukot. Essent. Fatty Acids
115
8-11
2016
Homo sapiens
brenda