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EC Tree
IUBMB Comments This bacterial enzyme acts on D-glucose, D-galactose, D-glucosides and D-galactosides, but the best substrates are disaccharides with a glucose moiety at the non-reducing end. It consists of two subunits, a catalytic subunit that contains an FAD cofactor and an iron-sulfur cluster, and a "hitch-hiker" subunit containing a signal peptide for translocation into the periplasm. A dedicated c-type cytochrome protein serves as an electron acceptor, transferring the electrons from the catalytic subunit to the cell's electron transfer chain. cf. EC 1.1.99.13, glucoside 3-dehydrogenase (acceptor).
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a D-glucoside
+
a ferric c-type cytochrome
=
a 3-dehydro-D-glucoside
+
a ferrous c-type cytochrome
Synonyms
d-aldohexopyranoside:cytochrome c oxidoreductase,
more
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D-aldohexopyranoside dehydrogenase
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ambiguous
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D-aldohexopyranoside:cytochrome c oxidoreductase
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D-aldohexoside:cytochrome c oxidoreductase
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D-glucoside 3-dehydrogenase
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ambiguous
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hexopyranoside-cytochrome c oxidoreductase
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Atu4377
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glucose 3-dehydrogenase
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glucose 3-dehydrogenase
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a D-glucoside + a ferric c-type cytochrome = a 3-dehydro-D-glucoside + a ferrous c-type cytochrome
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a D-glucoside:ferric c-type cytochrome 3-oxidoreductase
This bacterial enzyme acts on D-glucose, D-galactose, D-glucosides and D-galactosides, but the best substrates are disaccharides with a glucose moiety at the non-reducing end. It consists of two subunits, a catalytic subunit that contains an FAD cofactor and an iron-sulfur cluster, and a "hitch-hiker" subunit containing a signal peptide for translocation into the periplasm. A dedicated c-type cytochrome protein serves as an electron acceptor, transferring the electrons from the catalytic subunit to the cell's electron transfer chain. cf. EC 1.1.99.13, glucoside 3-dehydrogenase (acceptor).
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1,5-anhydro-D-glucitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-3-dehydro-D-glucose + reduced phenazine methosulfate
alpha-methyl-D-glucoside + acceptor
3-keto-alpha-methyl-glucoside + reduced acceptor
D-galactose + phenazine methosulfate
3-dehydro-D-galactose + reduced phenazine methosulfate
D-glucose + phenazine methosulfate
3-dehydro-D-gluose + reduced phenazine methosulfate
methyl alpha-D-glucoside + 2,6-dichlorophenolindophenol
methyl alpha-D-3-oxoglucoside + reduced 2,6-dichlorophenolindophenol
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?
methyl alpha-D-glucoside + cytochrome c
methyl alpha-D-3-oxoglucoside + reduced cytochrome c
methyl alpha-D-glucoside + cytochrome c551
methyl alpha-D-3-oxoglucoside + ferrous cytochrome c551
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substrate cytochrome c551 has a molecular mass of 15500
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-
?
methyl alpha-D-glucoside + phenazine methosulfate
methyl alpha-D-3-oxoglucoside + reduced phenazine methosulfate
sucrose + acceptor
3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor
additional information
?
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1,5-anhydro-D-glucitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
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-
-
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?
1,5-anhydro-D-glucitol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
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-
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?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-3-dehydro-D-glucose + reduced phenazine methosulfate
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?
2-deoxy-D-glucose + phenazine methosulfate
2-deoxy-3-dehydro-D-glucose + reduced phenazine methosulfate
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?
alpha-methyl-D-glucoside + acceptor
3-keto-alpha-methyl-glucoside + reduced acceptor
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ability to induce glucoside 3-dehydrogenase
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?
alpha-methyl-D-glucoside + acceptor
3-keto-alpha-methyl-glucoside + reduced acceptor
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ability to induce glucoside 3-dehydrogenase
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-
?
D-galactose + phenazine methosulfate
3-dehydro-D-galactose + reduced phenazine methosulfate
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-
?
D-galactose + phenazine methosulfate
3-dehydro-D-galactose + reduced phenazine methosulfate
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-
-
?
D-glucose + phenazine methosulfate
3-dehydro-D-gluose + reduced phenazine methosulfate
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-
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?
D-glucose + phenazine methosulfate
3-dehydro-D-gluose + reduced phenazine methosulfate
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?
lactose + acceptor
?
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ability to induce glucoside 3-dehydrogenase, massive production of glucoside 3-dehydrogenase by using minimal medium containing 0.8%, w/v, lactose
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-
?
lactose + acceptor
?
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ability to induce glucoside 3-dehydrogenase, massive production of glucoside 3-dehydrogenase by using minimal medium containing 0.8%, w/v, lactose
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?
maltose + acceptor
?
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no inducer for glucoside 3-dehydrogenase
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?
maltose + acceptor
?
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no inducer for glucoside 3-dehydrogenase
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?
methyl alpha-D-glucoside + cytochrome c
methyl alpha-D-3-oxoglucoside + reduced cytochrome c
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-
-
?
methyl alpha-D-glucoside + cytochrome c
methyl alpha-D-3-oxoglucoside + reduced cytochrome c
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-
-
?
methyl alpha-D-glucoside + phenazine methosulfate
methyl alpha-D-3-oxoglucoside + reduced phenazine methosulfate
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-
-
?
methyl alpha-D-glucoside + phenazine methosulfate
methyl alpha-D-3-oxoglucoside + reduced phenazine methosulfate
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-
-
?
sucrose + acceptor
3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor
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no inducer for glucoside 3-dehydrogenase
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-
?
sucrose + acceptor
3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + reduced acceptor
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no inducer for glucoside 3-dehydrogenase
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?
additional information
?
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no substrate: 3-O-methyl-D-glucose
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additional information
?
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no substrate: 3-O-methyl-D-glucose
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methyl alpha-D-glucoside + cytochrome c551
methyl alpha-D-3-oxoglucoside + ferrous cytochrome c551
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substrate cytochrome c551 has a molecular mass of 15500
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?
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[3Fe-4S]-center
the catalytic subunit contains an 3Fe-4S iron-sulfur cluster that acts as an electron acceptor for electrons from FAD in the oxidative half reaction
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additional information
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not inhibitory: EDTA
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6.6
1,5-anhydro-D-glucitol
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pH 8, 37°C
0.0034
cytochrome c
pH 7, 23°C
5.5
D-glucose
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pH 8, 37°C
3.2
methyl alpha-D-glucoside
pH 7, 23°C
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0.56
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carbon source: alpha-methyl-D-glucoside
0.74
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carbon source: isopropyl-thiogalactopyranoside
0.86
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carbon source: lactose
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i.e. catalytic subunit I, Gtd1
UniProt
brenda
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brenda
obsolete genus name: Deleya
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brenda
obsolete genus name: Deleya
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brenda
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brenda
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brenda
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brenda
i.e. catalytic subunit I, Gtd1
UniProt
brenda
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substrate cytochrome c551 is membrane-bound
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brenda
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brenda
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brenda
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metabolism
In the catalytic subunit, the reductive half reaction occurs using FAD as the electron acceptor, and the 3Fe-4S iron sulfur cluster then accepts the electron from reduced FAD. The reduced iron-sulfur cluster transfers the electron to the external cytochrome c-like molecule
metabolism
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In the catalytic subunit, the reductive half reaction occurs using FAD as the electron acceptor, and the 3Fe-4S iron sulfur cluster then accepts the electron from reduced FAD. The reduced iron-sulfur cluster transfers the electron to the external cytochrome c-like molecule
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A9CGJ1_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
561
0
63350
TrEMBL
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?
x * 63350, catalytic subunit I, calculated from sequence
?
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x * 63350, catalytic subunit I, calculated from sequence
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?
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x * 67000, SDS-PAGE
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monomer
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1 * 67000
additional information
enzyme is composed of the G3DH catalytic subunit I, G3DH hitch-hiker subunit II, and cytochrome c like molecule CYTc
additional information
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enzyme is composed of the G3DH catalytic subunit I, G3DH hitch-hiker subunit II, and cytochrome c like molecule CYTc
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recombinant catalytic subunit I and G3DH hitch-hiker subunit II, purified by Ni2+ affinity chromatography followed by anion exchange chromatography
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expression in Escherichia coli
gene encoding glucose 3-dehydrogenase cloned and expressed in Escherichia coli, open reading frame of 1686 nucleotides, FAD binding motif found in the N-terminal region of the gene
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expression is induced by growth on cellobiose, alpha-methylglucoside, 3-methylglucoside, kojibiose, and sophorose. Induction by sucrose, maltose, alpha,alpha-trehalose, melibiose, and lactose is weak. ACO induction is not repressed by D-glucose, it is repressed by succinate, malate, and fumarate
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Kojima, K.; Tsugawa, W.; Hamahuji, T.; Watazu, Y.; Sode, K.
Effect of growth substrates on production of new soluble glucose 3-dehydrogenase in Halomonas (Deleya) sp. alpha-15
Appl. Biochem. Biotechnol.
77-79
827-834
1999
Halomonas sp., Halomonas sp. alpha-15
brenda
Tsugawa, W.; Horiuchi, S.; Tanaka, M.; Wake, H.; Sode, K.
Purification of a marine bacterial glucose dehydrogenase from Cytophaga marinoflava and its application for measurement of 1,5-anhydro-D-glucitol
Appl. Biochem. Biotechnol.
56
301-310
1996
Leeuwenhoekiella marinoflava, Leeuwenhoekiella marinoflava IFO 14170
brenda
Miyazaki, R.; Yamazaki, T.; Yoshimatsu, K.; Kojima, K.; Asano, R.; Sode, K.; Tsugawa, W.
Elucidation of the intra- and inter-molecular electron transfer pathways of glucoside 3-dehydrogenase
Bioelectrochemistry
122
115-122
2018
Agrobacterium fabrum (A9CGJ1), Agrobacterium fabrum C58 (A9CGJ1)
brenda
Nakamura, L.; Tyler, D.
Induction of D aldohexoside cytochrome c oxidoreductase in Agrobacterium tumefaciens
J. Bacteriol.
129
830-835
1977
Agrobacterium fabrum
brenda
Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.
Physiological role of glucoside 3-dehydrogenase and cytochrome c551 in the sugar oxidizing system of Flavobacterium saccharophilum
J. Biochem.
103
938-943
1988
Flavobacterium saccharophilum
brenda
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