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)
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
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-
Pentose phosphate pathway
-
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ketogluconate metabolism
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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; strain 81-176
Q0PB96 and Q0PB95
-
Manually annotated by BRENDA team
subunit Cj0414 and subunit Cj0415; strain 81-176
Q0PB96 and Q0PB95
-
Manually annotated by BRENDA team
NBRC 3271
-
-
Manually annotated by BRENDA team
-
-
-
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
-
-
-
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
-
prosthetic group
-
cytochrome c1
flavin
additional information
Q0PB96 and Q0PB95
a putative NAD, FAD binding site is located within the first 48 amino acids of Cj0415
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxogluconate
-
competitive
o-benzoquinone
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0.5 mM, complete inhibition
oxalate
oxamate
pyruvate
Quinacrine hydrochloride
-
1 mM, 10% loss of activity
Quinine hydrochloride
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
-
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
-
-
0.15
phenazine methosulfate
-
-
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 and Q0PB95
cells grown at 37C, Cj0415 mutant
0.0019
Q0PB96 and Q0PB95
cells grown at 42C, Cj0414 mutant
0.0026
Q0PB96 and Q0PB95
cells grown at 37C, Cj0414 mutant
0.0045
Q0PB96 and Q0PB95
cells grown at 42C, Cj0415 mutant
0.0141
Q0PB96 and Q0PB95
cells grown at 37C, wild type
0.0333
Q0PB96 and Q0PB95
cells grown at 42C, wild type
additional information
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
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 and Q0PB95
predicted, subunit Cj0414
8.8
Q0PB96 and 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
-
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 and 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
-
1 * 15500 + 1 * 52500 + 1 * 68000, SDS-PAGE
63700
Q0PB96 and Q0PB95
predicted, subunit Cj0415
64000
-
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
-
5C, 16 h, stable
389915
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
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
-10C, Tris buffer, pH 7.0, stable for several weeks
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4C, 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 and Q0PB95
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Cj0414 and Cj0415 are 3.4 and 2.9fold more highly expressed at 42C compared to 37C, respectively
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81-176cj0414
Q0PB96 and Q0PB95
mutant, lacking the expression of the Cj0414 subunit
81-176cj0415
Q0PB96 and 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 (1066 entries)
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