Information on EC 1.1.1.215 - gluconate 2-dehydrogenase

Word Map on EC 1.1.1.215
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.215
-
RECOMMENDED NAME
GeneOntology No.
gluconate 2-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-gluconate + NADP+ = 2-dehydro-D-gluconate + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ketogluconate metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
ketogluconate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
D-gluconate:NADP+ oxidoreductase
Also acts on L-idonate, D-galactonate and D-xylonate.
CAS REGISTRY NUMBER
COMMENTARY hide
68417-42-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
acetic acid bacteria
maximal formation at the end of exponential growth phase
-
-
Manually annotated by BRENDA team
Acetobacter ascendens
-
-
-
Manually annotated by BRENDA team
Brevibacterium ketosoreductum
-
-
-
Manually annotated by BRENDA team
strain 81-176
-
-
Manually annotated by BRENDA team
strain 81-176
-
-
Manually annotated by BRENDA team
constitutive expressed enzyme
-
-
Manually annotated by BRENDA team
the large subunit is encoded by gene gndL, the small subunit by gene gndS, and the cytochrome C subunit by gene gndC; strain IFO 3271, gene gndL encoding the large subunit of the enzyme
UniProt
Manually annotated by BRENDA team
the large subunit is encoded by gene gndL, the small subunit by gene gndS, and the cytochrome C subunit by gene gndC; strain IFO 3271, gene gndL encoding the large subunit of the enzyme
UniProt
Manually annotated by BRENDA team
no activity in a number of oxidative or aerobic bacteria
-
-
-
Manually annotated by BRENDA team
strain Westling
-
-
Manually annotated by BRENDA team
strain Westling
-
-
Manually annotated by BRENDA team
CHA0
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
show the reaction diagram
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
show the reaction diagram
2-keto-L-gulonate + NADPH
L-idonate + NADP+
show the reaction diagram
2-oxo-D-gluconate + NADH + H+
D-gluconate + NAD+
show the reaction diagram
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
show the reaction diagram
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
show the reaction diagram
5-keto-D-gluconate + NADPH
D-gluconate + NADP+
show the reaction diagram
acetaldehyde + NADPH + H+
ethanol + NADP+
show the reaction diagram
-
poor substrate
-
-
?
D-galactonate + NADP+
2-dehydro-D-galactonate + NADPH
show the reaction diagram
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
show the reaction diagram
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH + H+
show the reaction diagram
D-xylonate + NADPH
2-keto-D-xylonate + NADP+
show the reaction diagram
glyoxal + NADPH
?
show the reaction diagram
-
reduction at 33% the rate of 2-ketogluconate reduction
-
-
?
glyoxylate + NADPH
glycolate + NADP+
show the reaction diagram
-
reduction at 350% the rate of 2-ketogluconate reduction
-
?
hydroxypyruvate + NADPH
2,3-dihydroxypropanoate + NADP+
show the reaction diagram
-
reduction at 733% the rate of 2-keto-gluconate reduction
-
?
L-idonate + NADP+
2-keto-L-idonate + NADPH
show the reaction diagram
pyruvate + NADPH + H+
lactate + NADP+
show the reaction diagram
-
reduction at 7% the rate of 2-ketogluconate reduction
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,5-diketo-D-gluconate + NADPH
5-keto-D-gluconate + NADP+
show the reaction diagram
2-dehydro-D-gluconate + NADPH
D-gluconate + NADP+
show the reaction diagram
2-oxo-D-gluconate + NADPH + H+
D-gluconate + NADP+
show the reaction diagram
2-oxo-L-gulonate + NADPH + H+
L-idonate + NADP+
show the reaction diagram
D-gluconate + NADP+
2-dehydro-D-gluconate + NADPH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
NADP+
NADPH
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxamate
-
slight inhibition of reverse reaction
sulfhydryl reagents
Tartronate
-
slight inhibition of reverse reaction
additional information
-
not inhibited by monoiodoacetate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
expression and activity of cj0414 and cj0415 are higher at 42C than at 37C
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
2,5-diketo-D-gluconate
Brevibacterium ketosoreductum
-
-
16
2-keto-D-galactonate
-
-
5.3
2-keto-D-gluconate
Acetobacter ascendens
-
-
91
2-keto-L-gulonate
-
-
5.16
2-oxo-D-gluconate
pH 7.0, 25C
0.86
5-Keto-D-gluconate
-
-
2.4
D-gluconate
-
-
4.4
gluconate
Acetobacter ascendens
-
-
0.38
glyoxylate
-
-
0.065
Hydroxypyruvate
-
-
0.051
NADH
pH 7.0, 25C
0.083 - 1.2
NADP+
0.0074 - 0.71
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48.2
2-oxo-D-gluconate
Gluconobacter oxydans
Q5FTU6
pH 7.0, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.34
2-oxo-D-gluconate
Gluconobacter oxydans
Q5FTU6
pH 7.0, 25C
13115
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22.2
Brevibacterium ketosoreductum
-
-
137
purified native enzyme
187
Acetobacter ascendens
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
reduction of 2-ketogluconate
11
Acetobacter ascendens
-
oxidation of gluconate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
Acetobacter ascendens
-
about half-maximal activity at pH 4.5 and 8.5, reduction of ketogluconate
5 - 9.2
-
about half-maximal activity at pH 5.0 and 9.2, reduction of ketogluconate
10 - 12
Acetobacter ascendens
-
about half-maximal activity at pH 10 and 12, oxidation of gluconate
10.8 - 12.5
-
about half-maximal activity at pH 10.8 and 12.5, oxidation of gluconate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
Acetobacter ascendens
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 65
Acetobacter ascendens
-
about half-maximal activity at 35C and 65C
40 - 55
-
about half-maximal activity at 40C and 55C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
cj0414, isoelectric focusing
8.8
-
cj0415, isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
-
8 * 15000, SDS-PAGE
23000
1 * 23000 + 1 * 44000 + 1 * 65000, SDS-PAGE
26900
-
sequence analysis, cj0414
33200
6 * 33200, SDS-PAGE
34000
-
2 * 43000 + 1 * 34000, SDS-PAGE
35000
Brevibacterium ketosoreductum
-
2 * 35000, SDS-PAGE
36000
-
2 * 36000, SDS-PAGE
40000
Acetobacter ascendens
-
3 * 40000, SDS-PAGE
43000
-
2 * 43000 + 1 * 34000, SDS-PAGE
44000
1 * 23000 + 1 * 44000 + 1 * 65000, SDS-PAGE
63700
-
sequence analysis, cj0415
65000
1 * 23000 + 1 * 44000 + 1 * 65000, SDS-PAGE
72000
Brevibacterium ketosoreductum
-
gel filtration
74000
-
gel filtration
120000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
octamer
-
8 * 15000, SDS-PAGE
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
Brevibacterium ketosoreductum
-
35% of activity left after incubation at pH 8.4 for 2 h at 30C, no remaining activity below pH 5.2 or above pH 10.0
286278
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
Acetobacter ascendens
-
stable for 10 min, oxidation activity
53
Acetobacter ascendens
-
stable for 10 min, reduction activity
60
-
rapid inactivation
70
Acetobacter ascendens
-
stable for 10 min in the presence of either 2-ketogluconate or gluconate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-ketogluconate enhances thermal and storage stability even of dilute enzyme solutions, 0.1 mg protein/l
Acetobacter ascendens
-
2-mercaptoethanol stabilizes
-
5-ketogluconate does not stabilize
Acetobacter ascendens
-
dialysis leads to general loss of activity
-
dialysis, stable to
-
gluconate enhances thermal and storage stability even of dilute enzyme solutions, 0.1 mg protein/l
Acetobacter ascendens
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, crude extract stable for up to 7 days under nitrogen
-
-20C, stable in the presence of sulfhydryl agents and ammonium sulfate
-
0C, stable for at least a month in phosphate buffer
-
5C, stable in 0.01 M potassium phosphate buffer with the addition of 2-mercaptoethanol
ammonium sulfate solution of crystalline enzyme stable for over 2 years
Acetobacter ascendens
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on Blue-Dextran Sepharose B
Acetobacter ascendens
-
ammonium sulfate, DEAE-Toyopearl, Phenyl-Toyopearl, Blue-Sepharose, Sephacryl S-200
Brevibacterium ketosoreductum
-
His6-tagged enzyme, metal-chelate affinity chromatography
-
native enzyme 67fold from membranes and bound to FAD by solubilization with 0.1% Triton X-100, anion chromatography, and three steps of hydrophobic interaction chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant large subunits
DNA and amino acid sequence determination and analysis, overexpression of wild-type and expression of start codon mutated enzyme in Escherichia coli strain DH5alpha
expressed in Escherichia coli
-
expression in Escherichia coli
mutagenized cj0414 and cj0415 alleles are introduced into Campylobacter jejuni 81-176
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
Show AA Sequence (257 entries)
Please use the Sequence Search for a specific query.