Information on EC 1.1.99.3 - gluconate 2-dehydrogenase (acceptor)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.99.3
-
RECOMMENDED NAME
GeneOntology No.
gluconate 2-dehydrogenase (acceptor)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucose degradation (oxidative)
-
-
L-ascorbate biosynthesis VI (engineered pathway)
-
-
ketogluconate metabolism
-
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Pentose phosphate pathway
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
D-gluconate:acceptor 2-oxidoreductase
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-81-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit Cj0414 and subunit Cj0415
Q0PB96, Q0PB95
-
Manually annotated by BRENDA team
subunit Cj0414 and subunit Cj0415
Q0PB96, Q0PB95
-
Manually annotated by BRENDA team
NBRC 3271
-
-
Manually annotated by BRENDA team
NBRC 3271
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
ATCC 29267
-
-
Manually annotated by BRENDA team
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-
-
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
D-gluconate + 2,6-dichlorophenolindophenol
2-oxogluconate + ?
show the reaction diagram
D-gluconate + acceptor
2-dehydro-D-gluconate + reduced acceptor
show the reaction diagram
D-gluconate + acceptor
2-oxogluconate + reduced acceptor
show the reaction diagram
-
one of the key enzymes of gluconate catabolism
-
-
?
D-gluconate + coenzyme Q1
2-oxogluconate + ?
show the reaction diagram
-
-
-
-
?
D-gluconate + FAD
2-dehydro-D-gluconate + FADH2
show the reaction diagram
D-gluconate + ferricyanide
2-dehydro-D-gluconate + ferrocyanide
show the reaction diagram
-
-
-
-
?
D-gluconate + ferricyanide
2-oxogluconate + ferrocyanide
show the reaction diagram
D-gluconate + oxidized 2,6-dichlorophenolindophenol
2-dehydro-D-gluconate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
D-gluconate + phenazine methosulfate
2-oxogluconate + ?
show the reaction diagram
additional information
?
-
-
no activity with menadione
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-
-
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
D-gluconate + acceptor
2-dehydro-D-gluconate + reduced acceptor
show the reaction diagram
D-gluconate + acceptor
2-oxogluconate + reduced acceptor
show the reaction diagram
-
one of the key enzymes of gluconate catabolism
-
-
?
D-gluconate + FAD
2-dehydro-D-gluconate + FADH2
show the reaction diagram
D-gluconate + oxidized 2,6-dichlorophenolindophenol
2-dehydro-D-gluconate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8alpha-(N1-histidyl)-FAD
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prosthetic group
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cytochrome c1
flavin
additional information
Q0PB96; Q0PB95;
a putative NAD, FAD binding site is located within the first 48 amino acids of Cj0415
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxogluconate
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competitive
o-benzoquinone
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0.5 mM, complete inhibition
oxalate
oxamate
pyruvate
Quinacrine hydrochloride
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1 mM, 10% loss of activity
Quinine hydrochloride
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
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stimulates in presence of Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
2,6-dichlorophenolindophenol
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-
0.11
coenzyme Q1
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-
0.3 - 3.2
D-gluconate
2.5
ferricyanide
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-
0.15
phenazine methosulfate
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29 - 123
2-oxo-D-gluconate
2.8 - 2.9
oxalate
0.07 - 0.8
oxamate
4.6 - 18.3
pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0013
Q0PB96; Q0PB95;
cells grown at 37°C, Cj0415 mutant
0.0019
Q0PB96; Q0PB95;
cells grown at 42°C, Cj0414 mutant
0.0026
Q0PB96; Q0PB95;
cells grown at 37°C, Cj0414 mutant
0.0045
Q0PB96; Q0PB95;
cells grown at 42°C, Cj0415 mutant
0.0141
Q0PB96; Q0PB95;
cells grown at 37°C, wild type
0.0333
Q0PB96; Q0PB95;
cells grown at 42°C, wild type
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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reaction with coenzyme Q1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
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pH 4.0: about 40% of maximal activity, pH 6.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
Q0PB96; Q0PB95;
predicted, subunit Cj0414
8.8
Q0PB96; Q0PB95;
predicted, subunit Cj0415
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15500
-
1 * 15500 + 1 * 52500 + 1 * 68000, SDS-PAGE
21000
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1 * 21000 + 1 * 45000 + 1 * 64000, SDS-PAGE
21700
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1 * 21700 + 1 * 47500 + 1 * 66500, SDS-PAGE
24000
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1 * 24000, subunit of unknown function, + 1 * 47000, cytochrome c subunit, + 1 * 68000, dehydrogenase subunit, calculation from nucleotide sequence, SDS-PAGE
26900
Q0PB96; Q0PB95;
predicted, subunit Cj0414
45000
-
1 * 21000 + 1 * 45000 + 1 * 64000, SDS-PAGE
47000
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1 * 24000, subunit of unknown function, + 1 * 47000, cytochrome c subunit, + 1 * 68000, dehydrogenase subunit, calculation from nucleotide sequence, SDS-PAGE
47500
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1 * 21700 + 1 * 47500 + 1 * 66500, SDS-PAGE
50000
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1 * 22000, subunit of unclear function, + 1 * 50000, cytochrome c1, + 1 * 66000, flavoprotein, SDS-PAGE
52000
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1 * 22000 + 1 * 52000 + 1 * 66000, SDS-PAGE
52500
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1 * 15500 + 1 * 52500 + 1 * 68000, SDS-PAGE
63700
Q0PB96; Q0PB95;
predicted, subunit Cj0415
64000
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1 * 21000 + 1 * 45000 + 1 * 64000, SDS-PAGE
66500
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1 * 21700 + 1 * 47500 + 1 * 66500, SDS-PAGE
124000 - 131000
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sucrose density gradient centrifugation
132000 - 138000
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non-denaturing PAGE
136000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
trimer
additional information
-
in absence of Triton X-100 the enzyme becomes dimeric
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
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5°C, 16 h, stable
389915
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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10 min, stable below
60
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10 min, about 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against distilled water causes gradual loss of activity after 8 to 10 h. Dialysis against neutral phosphate buffer or Tris buffer for 24 h in the cold does not produce a loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, Tris buffer, pH 7.0, stable for several weeks
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4°C, Tris buffer, pH 7.0, stable for 3-4 days
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase
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into the pGEM-T easy vector for sequencing
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the cj0414-cj0415 PCR product is subcloned into pCRII-TOPO, cj0414 and cj0415 are cloned into the vector pBluescript II
Q0PB96; Q0PB95;
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cj0414 and Cj0415 are 3.4 and 2.9fold more highly expressed at 42°C compared to 37°C, respectively
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81-176cj0414
Q0PB96; Q0PB95;
mutant, lacking the expression of the Cj0414 subunit
81-176cj0415
Q0PB96; Q0PB95;
mutant, lacking the expression of the Cj0415 subunit
81-176cj0414
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mutant, lacking the expression of the Cj0414 subunit
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81-176cj0415
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mutant, lacking the expression of the Cj0415 subunit
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Show AA Sequence (1183 entries)
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