Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + 7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + 7alpha-hydroxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cholesterol hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cholesterol hydroxide
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + linoleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + oleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + oleic acid
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butanol
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + trans-pinocarveylhydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + trans-pinocarveyl alcohol
-
-
-
?
cumene hydroperoxide + dihydrolipoamide
2-phenylpropan-2-ol + lipoamide
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
H2O2 + dihydrolipoamide
H2O + lipoamide
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
linoleic acid hydroperoxide + dihydrolipoamide
? + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
linoleic acid hydroperoxide + reduced dithiothreitol
? + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
tert-butyl hydroperoxide + dihydrolipoamide
tert-butanol + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
additional information
?
-
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + 7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + 7alpha-hydroxy-3beta-hydroxycholest-6-ene
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + 7alpha-hydroperoxy-3beta-hydroxycholest-6-ene
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + 7alpha-hydroxy-3beta-hydroxycholest-6-ene
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cholesterol hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cholesterol hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cholesterol hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cholesterol hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
best substrate for AhpD
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
best substrate for AhpD
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + cumene hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + cumene hydroxide
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + 2 H2O
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + linoleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ?
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + linoleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ?
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + oleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + oleic acid
poor substrate
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + oleic acid hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + oleic acid
poor substrate
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + ROOH
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + ROH
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butanol
fatty acid (but not cholesterol) hydroperoxides dock well into the active site of Ohr from Xylella fastidiosa and are efficiently reduced by the recombinant enzyme
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butanol
fatty acid (but not cholesterol) hydroperoxides dock well into the active site of Ohr from Xylella fastidiosa and are efficiently reduced by the recombinant enzyme
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
a [lipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
cumene hydroperoxide + dihydrolipoamide
2-phenylpropan-2-ol + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
cumene hydroperoxide + dihydrolipoamide
2-phenylpropan-2-ol + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
cumene hydroperoxide + dithiothreitol
2-phenylpropan-2-ol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O2 + dihydrolipoamide
H2O + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O2 + dihydrolipoamide
H2O + lipoamide
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
H2O2 + reduced dithiothreitol
H2O + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
lipoamide + H2O2
? + H2O
-
-
-
?
lipoamide + H2O2
? + H2O
-
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
tert-butyl hydroperoxide + reduced dithiothreitol
tert-butanol + oxidized dithiothreitol
the peroxidase activity of the enzyme (MfOhr) is supported by dithiothreitol or dihydrolipoamide, but not by beta-mercaptoethanol or glutathione. MfOhr displays preference for organic hydroperoxides (cumene hydroperoxide and tert-butyl hydroperoxide) over hydrogen peroxide. MfOhr presents extraordinary reactivity towards linoleic acid hydroperoxides
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from alpha-ketoglutarate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine + tert-butyl hydroperoxide
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O + tert-butyl alcohol
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-[(R)-dihydrolipoyl]-L-lysine + H2O2
[dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complex]-N6-lipoyl-L-lysine + H2O
-
-
-
?
additional information
?
-
-
AhpD directly interacts with AhpC as an electron donor, and the conserved Cys residues in active site of AhpD are important for enzyme reduction
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
additional information
?
-
AhpD contributes to regenerate a variety of thiol-dependent peroxidase in the decomposition of peroxide by linking a dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide succinyltransferase (SucB)/NADH system through the cyclization of their own active site dithiol to the oxidized disulphide. The CXXC motif of AhpD is essential to maintain the peroxides reduction activity of thiol-dependent peroxidase. The AhpD system is an important redox system in cells besides the thioredoxin system. Corynebacterium glutamicum AhpD not only has the ability to reduce a variety of thioredoxin-dependent antioxidant enzymes, including mycothiol peroxidase, peroxiredoxin, and Ohr (organic Hydroperoxide Resistance), but also shows a higher affinity for Ohr than those of mycothiol peroxidase and peroxiredoxin, which is different from the only AhpC-reducing Mycobacterium tuberculosis AhpD
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
drug target
immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract. AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which could provide a practical strategy for the prevention of colorectal cancer associated with Fn infection
drug target
-
immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract. AhpC as a potential vaccine candidate against inhabitation or infection of Fusobacterium nucleatum in the intestinal tract, which could provide a practical strategy for the prevention of colorectal cancer associated with Fn infection
-
malfunction
DELTAahpCD strain is notably more sensitive than its parent strain to hydrogen peroxide (H2O2) but not to organic peroxides (tertbutyl hydroperoxide and cumene hydroperoxide), in the early log phase. The catalase activity of the DELTAahpCD strain is affected at a relatively low level of H2O2 stress. The DELTAahpCD strain induces a reduced number of stem nodules in Sesbania rostrata with lowering of nitrogenase activity
malfunction
DELTAahpD1DELTAahpD2 mutants exhibit significantly decreased resistance to adverse stress conditions and increased accumulation of reactive oxygen species (ROS)
malfunction
DELTAohr strain presents a reduced capacity to grow in the presence of either artificial (cumene hydroperoxide and tert-butyl hydroperoxide) or fatty acid hydroperoxides compared with the wild type
malfunction
-
DELTAahpCD strain is notably more sensitive than its parent strain to hydrogen peroxide (H2O2) but not to organic peroxides (tertbutyl hydroperoxide and cumene hydroperoxide), in the early log phase. The catalase activity of the DELTAahpCD strain is affected at a relatively low level of H2O2 stress. The DELTAahpCD strain induces a reduced number of stem nodules in Sesbania rostrata with lowering of nitrogenase activity
-
malfunction
-
DELTAahpD1DELTAahpD2 mutants exhibit significantly decreased resistance to adverse stress conditions and increased accumulation of reactive oxygen species (ROS)
-
malfunction
-
DELTAohr strain presents a reduced capacity to grow in the presence of either artificial (cumene hydroperoxide and tert-butyl hydroperoxide) or fatty acid hydroperoxides compared with the wild type
-
physiological function
AhpC is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
physiological function
AhpD is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
physiological function
Mycobacterium tuberculosis persists in host macrophages, where it faces a nutrient-poor environment and is exposed to oxidative and nitrosative stress. The enzyme defends Mycobacterium tuberculosis against oxidative stress
physiological function
the enzyme provides antioxidant protection
physiological function
AhpCD is required for resistance to low concentrations of H2O2 in the free-living stage and during symbiosis with Sesbania rostrata. AhpCD contributes to H2O2 resistance at the early log phase of Azorhizobium caulinodans growth. ahpCD is required for stem nodulation but not root nodulation in Sesbania rostrata
physiological function
AhpD acts as a backup of thioredoxin to provide reducing power for peroxidase
physiological function
-
alkyl hydroperoxide reductase subunit C acquires chaperone activity under heat stress. High-molecular-weight oligomer formation and the chaperone-like activity of oxidized AhpC depend on the incubation temperature and the period of incubation
physiological function
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite
physiological function
the ahpD gene is more involved in defences against H2O2 than in detoxifying alkyl hydroperoxide. It plays an important role in hydrogen peroxide-induced oxidative stress response
physiological function
the enzyme is involved in the Pseudomonas aeruginosa response to fatty acid hydroperoxides and to peroxynitrite. Therefore, Ohr plays central roles in the bacterial response to two hydroperoxides that are at the host-pathogen interface
physiological function
the enzyme is important for H2O2 detoxification in vitro and also critical for symbiosis of Azorhizobium caulinodans with Sesbania rostrate. The enzyme is required for stem nodulation and nitrogenase activity
physiological function
-
AhpCD is required for resistance to low concentrations of H2O2 in the free-living stage and during symbiosis with Sesbania rostrata. AhpCD contributes to H2O2 resistance at the early log phase of Azorhizobium caulinodans growth. ahpCD is required for stem nodulation but not root nodulation in Sesbania rostrata
-
physiological function
-
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite
-
physiological function
-
the ahpD gene is more involved in defences against H2O2 than in detoxifying alkyl hydroperoxide. It plays an important role in hydrogen peroxide-induced oxidative stress response
-
physiological function
-
AhpD acts as a backup of thioredoxin to provide reducing power for peroxidase
-
physiological function
-
Mycobacterium tuberculosis persists in host macrophages, where it faces a nutrient-poor environment and is exposed to oxidative and nitrosative stress. The enzyme defends Mycobacterium tuberculosis against oxidative stress
-
physiological function
-
the enzyme provides antioxidant protection
-
physiological function
-
AhpD is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
-
physiological function
-
AhpC is a critical element of the antioxidant defense system of Mycobacterium tuberculosis
-
physiological function
-
the enzyme is important for H2O2 detoxification in vitro and also critical for symbiosis of Azorhizobium caulinodans with Sesbania rostrate. The enzyme is required for stem nodulation and nitrogenase activity
-
physiological function
-
the enzyme is involved in the Pseudomonas aeruginosa response to fatty acid hydroperoxides and to peroxynitrite. Therefore, Ohr plays central roles in the bacterial response to two hydroperoxides that are at the host-pathogen interface
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Shi, S.; Ehrt, S.
Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis
Infect. Immun.
74
56-63
2006
Mycobacterium tuberculosis (P9WQB5), Mycobacterium tuberculosis (P9WQB7), Mycobacterium tuberculosis ATCC 25618 (P9WQB5), Mycobacterium tuberculosis ATCC 25618 (P9WQB7)
brenda
Hillas, P.J.; del Alba, F.S.; Oyarzabal, J.; Wilks, A.; Ortiz De Montellano, P.R.
The AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosis
J. Biol. Chem.
275
18801-18809
2000
Mycobacterium tuberculosis (P9WQB5), Mycobacterium tuberculosis (P9WQB7), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WQB5), Mycobacterium tuberculosis ATCC 25618 (P9WQB7)
brenda
Koshkin, A.; Nunn, C.M.; Djordjevic, S.; Ortiz de Montellano, P.R.
The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics
J. Biol. Chem.
278
29502-29508
2003
Mycobacterium tuberculosis (P9WQB5), Mycobacterium tuberculosis ATCC 25618 (P9WQB5)
brenda
Cussiol, J.R.; Alegria, T.G.; Szweda, L.I.; Netto, L.E.
Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase
J. Biol. Chem.
285
21943-21950
2010
Xylella fastidiosa (Q9PCF4), Xylella fastidiosa 9a5c (Q9PCF4)
brenda
Jiang, G.; Yang, J.; Li, X.; Cao, Y.; Liu, X.; Ling, J.; Wang, H.; Zhong, Z.; Zhu2, J.
Alkyl hydroperoxide reductase is important for oxidative stress resistance and symbiosis in Azorhizobium caulinodans
FEMS Microbiol. Lett.
366
fnz014
2019
Azorhizobium caulinodans (A8HQP5), Azorhizobium caulinodans (A8HQP9 AND A8HQP5), Azorhizobium caulinodans, Azorhizobium caulinodans ORS 571 (A8HQP9 AND A8HQP5), Azorhizobium caulinodans ORS571 (A8HQP5)
brenda
Hong, E.; Jeong, H.; Lee, D.; Kim, Y.; Lee, H.
The ahpD gene of Corynebacterium glutamicum plays an important role in hydrogen peroxide-induced oxidative stress response
J. Biochem.
165
197-204
2019
Corynebacterium glutamicum (Q8NMX8), Corynebacterium glutamicum ATCC 13032 (Q8NMX8)
brenda
Su, T.; Si, M.; Zhao, Y.; Yao, S.; Che, C.; Liu, Y.; Chen, C.
Function of alkyl hydroperoxidase AhpD in resistance to oxidative stress in Corynebacterium glutamicum
J. Gen. Appl. Microbiol.
65
72-79
2019
Corynebacterium glutamicum (Q8NMX8), Corynebacterium glutamicum (Q8NN44), Corynebacterium glutamicum ATCC 13032 (Q8NMX8), Corynebacterium glutamicum ATCC 13032 (Q8NN44)
brenda
Alegria, T.; Meireles, D.; Cussiol, J.; Hugo, M.; Trujillo, M.; De Oliveira, M.; Miyamoto, S.; Queiroz, R.; Valadares, N.; Garratt, R.; Radi, R.; Di Mascio, P.; Augusto, O.; Netto, L.
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite
Proc. Natl. Acad. Sci. USA
114
E132-E141
2017
Pseudomonas aeruginosa (A0A0H2ZCJ7), Xylella fastidiosa (Q9PCF4), Xylella fastidiosa, Xylella fastidiosa 9a5c (Q9PCF4), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZCJ7)
brenda
Meireles, D.; Domingos, R.; Gaiarsa, J.; Ragnoni, E.; Bannitz-Fernandes, R.; da Silva Neto, J.; de Souza, R.; Netto, L.
Functional and evolutionary characterization of Ohr proteins in eukaryotes reveals many active homologs among pathogenic fungi
Redox Biol.
12
600-609
2017
Pseudocercospora fijiensis (N1Q9R6), Pseudocercospora fijiensis, Pseudocercospora fijiensis CIRAD86 (N1Q9R6)
brenda
Guo, S.H.; Wang, H.F.; Nian, Z.G.; Wang, Y.D.; Zeng, Q.Y.; Zhang, G.
Immunization with alkyl hydroperoxide reductase subunit C reduces Fusobacterium nucleatum load in the intestinal tract
Sci. Rep.
7
10566
2017
Fusobacterium nucleatum (Q8R6D3), Fusobacterium nucleatum subsp. nucleatum (Q8R6D3), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 (Q8R6D3), Fusobacterium nucleatum ATCC 25586 (Q8R6D3)
brenda
Kamariah, N.; Eisenhaber, B.; Eisenhaber, F.; Grber, G.
Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions
Sci. Rep.
8
14151
2018
Escherichia coli
brenda
Zhang, B.; Gu, H.; Yang, Y.; Bai, H.; Zhao, C.; Si, M.; Su, T.; Shen, X.
Molecular mechanisms of AhpC in resistance to oxidative stress in Burkholderia thailandensis
Front. Microbiol.
10
1483
2019
Burkholderia thailandensis
brenda