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Information on EC 1.1.99.4 - dehydrogluconate dehydrogenase
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1.1.99.4 dehydrogluconate dehydrogenaseIUBMB Comments
A flavoprotein.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2-keto-D-gluconate dehydrogenase, 2-keto-gluconate dehydrogenase, 2-oxogluconate dehydrogenase, 2KGDH, alpha-ketogluconate dehydrogenase, dehydrogenase, ketogluconate, ketogluconate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-keto-D-gluconate dehydrogenase
-
-
-
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2-keto-gluconate dehydrogenase
2-oxogluconate dehydrogenase
-
-
-
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2KGDH
alpha-ketogluconate dehydrogenase
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-
-
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dehydrogenase, ketogluconate
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-
-
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ketogluconate dehydrogenase
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-
-
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2-keto-gluconate dehydrogenase
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
-
-
2KGDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-dehydro-D-gluconate + acceptor = 2,5-didehydro-D-gluconate + reduced acceptor
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
-
-
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
2-dehydro-D-gluconate:acceptor 2-oxidoreductase
A flavoprotein.
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CAS REGISTRY NUMBER
COMMENTARY
9028-82-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dehydro-D-gluconate + methylene blue
2,5-didehydro-D-gluconate + ?
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methylene blue is not as effective as 2,6-dichlorophenolindophenol
-
-
?
2-dehydro-D-gluconate + nitro blue tetrazolium
2,5-didehydro-D-gluconate + ?
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-
-
-
?
2-dehydro-D-gluconate + phenazine methosulfate
2,5-didehydro-D-gluconate + ?
-
-
-
-
?
2-dehydro-D-gluconate + pyocyanine
2,5-didehydro-D-gluconate + ?
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pyocyanine is not as effective as 2,6-dichlorophenolindophenol
-
-
?
2-dehydro-D-gluconate + 2,6-dichlorophenolindophenol
2,5-didehydro-D-gluconate + ?
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-
-
-
?
2-dehydro-D-gluconate + 2,6-dichlorophenolindophenol
2,5-didehydro-D-gluconate + ?
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-
-
-
?
2-dehydro-D-gluconate + 2,6-dichlorophenolindophenol
2,5-didehydro-D-gluconate + ?
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-
-
-
?
2-dehydro-D-gluconate + 2,6-dichlorophenolindophenol
2,5-didehydro-D-gluconate + ?
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-
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme is the primary dehydrogenase of the 2-keto-D-gluconate oxidizing system
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + ferricyanide
2,5-didehydro-D-gluconate + ferrocyanide
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-
-
-
?
2-dehydro-D-gluconate + ferricyanide
2,5-didehydro-D-gluconate + ferrocyanide
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
-
-
-
?
2-dehydro-D-gluconate + ferricyanide
2,5-didehydro-D-gluconate + ferrocyanide
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
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-
-
?
2-dehydro-D-gluconate + ferricyanide
2,5-didehydro-D-gluconate + ferrocyanide
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-
-
-
?
additional information
?
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A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
the enzyme is completely inert toward 5-oxoglutarate, D-gluconate, D-glucose, D-sorbitol, L-lactate, L-malate, and D-fructose
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additional information
?
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the enzyme is completely inert toward 5-oxoglutarate, D-gluconate, D-glucose, D-sorbitol, L-lactate, L-malate, and D-fructose
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-
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additional information
?
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A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
the enzyme is completely inert toward 5-oxoglutarate, D-gluconate, D-glucose, D-sorbitol, L-lactate, L-malate, and D-fructose
-
-
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additional information
?
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the enzyme is completely inert toward 5-oxoglutarate, D-gluconate, D-glucose, D-sorbitol, L-lactate, L-malate, and D-fructose
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-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme is the primary dehydrogenase of the 2-keto-D-gluconate oxidizing system
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
2-dehydro-D-gluconate + acceptor
?
-
enzyme of the D-glucose oxidation pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome
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contains 0.91 mol of tightly bound c-type cytochrome per mol of enzyme
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flavin
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contains 8alpha-(N3-histidyl) riboflavin in the dinucleotide form; flavoprotein
flavin
-
contains 0.44 mol of covalently bound flavin per mol of enzyme; flavoprotein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cytochrome c subunit and large subunit and small subunit
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
UniProt
brenda
cytochrome c subunit and large subunit and small subunit
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A0L0MEH6_9BURK
188
1
20118
TrEMBL
A0A3S4GEN8_YEREN
143
0
16043
TrEMBL
A0A447RGE1_YEREN
366
0
40433
TrEMBL
A0A4U9IU42_YEREN
169
1
18525
TrEMBL
A0A0H3P0D0_YERE1
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
169
1
18513
TrEMBL
A0A0H3NSN4_YERE1
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
531
0
58797
TrEMBL
A0A1B7KFI7_9GAMM
534
0
59001
TrEMBL
E5AVE0_PARRH
Paraburkholderia rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
161
0
17120
TrEMBL
A0A0H3NXJ5_YERE1
Yersinia enterocolitica subsp. palearctica serotype O:3 (strain DSM 13030 / CIP 106945 / Y11)
422
1
46398
TrEMBL
A0A3S4KB72_YEREN
169
1
18513
TrEMBL
A0A0H3C822_CAUVN
Caulobacter vibrioides (strain NA1000 / CB15N)
579
0
64397
TrEMBL
W0HNP6_9GAMM
447
0
47629
TrEMBL
A0A1B7KFJ3_9GAMM
449
1
47439
TrEMBL
A0A4U9IWK2_YEREN
539
0
59559
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
-
1 * 61000, flavoprotein + 1 * 47000, cytochrome component, + 1 * 25000, function unclear, SDS-PAGE
47000
-
1 * 61000, flavoprotein + 1 * 47000, cytochrome component, + 1 * 25000, function unclear, SDS-PAGE
61000
-
1 * 61000, flavoprotein + 1 * 47000, cytochrome component, + 1 * 25000, function unclear, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
trimer
-
1 * 61000, flavoprotein + 1 * 47000, cytochrome component, + 1 * 25000, function unclear, SDS-PAGE
trimer
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
a small subunit, a large subunit, and a cytochrome c subunit
trimer
-
a small subunit, a large subunit, and a cytochrome c subunit
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Gluconobacter japonicas strain NBRC3271
A0A0B6VQJ4; A0A0B6VN56; A0A0B6VKP6
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Datta, A.G.; Katznelson, H.
The oxidation of 2-ketogluconate by a partially purified enzyme from Acetobacter melanogenum
Arch. Biochem. Biophys.
65
576-578
1956
Gluconobacter oxydans
brenda
Bouvet, O.M.M.; Lenormand, P.; Grimont, P.A.D.
Taxonomic diversity of the D-glucose oxidation pathway in the Enterobacteriaceae
Int. J. Syst. Bacteriol.
39
61-67
1989
Ewingella americana, Pantoea cypripedii, Rahnella aquatilis, Serratia grimesii, Serratia liquefaciens, Serratia marcescens, Shimwellia blattae, Tatumella ptyseos
-
brenda
McIntire, W.; Singer, T.P.; Ameyama, M.; Adachi, O.; Matsushita, K.; Shinagawa, E.
Identification of the covalently bound flavins of D-gluconate dehydrogenases from Pseudomonas aeruginosa and Pseudomonas fluorescens and of 2-keto-D-gluconate dehydrogenase from Gluconobacter melanogenus
Biochem. J.
231
651-654
1985
Gluconobacter oxydans
brenda
Ameyama, M.
Enzymic microdetermination of D-glucose, D-fructase, D-gluconate, 2-keto-D-gluconate, aldehyde, and alcohol with membrane-bound dehydrogenase
Methods Enzymol.
89
20-29
1982
Gluconobacter sp.
-
brenda
Shinagawa, E.; Ameyama, M.
2-Keto-D-gluconate dehydrogenase from Gluconobacter melanogenum, membrane-bound
Methods Enzymol.
89
194-198
1982
Gluconobacter oxydans
-
brenda
Shinagawa, E.; Matsushita, K.; Adachi, O.; Ameyama, M.
Purification and characterization of 2-keto-D-gluconate dehydrogenase from Gluconobacter melanogenus
Agric. Biol. Chem.
45
1079-1085
1981
Gluconobacter oxydans
-
brenda
Shinagawa, E.; Chiyonobu, T.; Adachi, O.; Ameyama, M.
Distribution and solubilization of particulate gluconate dehydrogenase in acetic acid bacteria
Agric. Biol. Chem.
40
475-483
1976
Frateuria aurantia, Gluconacetobacter liquefaciens, Gluconobacter oxydans, Gluconobacter sphaericus
-
brenda
Kataoka, N.; Matsutani, M.; Yakushi, T.; Matsushita, K.
Efficient production of 2,5-diketo-D-gluconate via heterologous expression of 2-ketogluconate dehydrogenase in Gluconobacter japonicus
Appl. Environ. Microbiol.
81
3552-3560
2015
Gluconobacter oxydans (A0A0B6VQJ4 and A0A0B6VN56 and A0A0B6VKP6), Gluconobacter oxydans, Gluconobacter oxydans NBRC3293 (A0A0B6VQJ4 and A0A0B6VN56 and A0A0B6VKP6), Gluconobacter oxydans NBRC3293
brenda
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