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Enzyme Nomenclature
Information on EC 1.2.1.26 - 2,5-dioxovalerate dehydrogenase
for references in articles please use BRENDA:EC1.2.1.26
Word Map on EC 1.2.1.26
- 1.2.1.26
-
dehydratase
-
azospirillum
- l-arabinose
- degradation
-
aldolase
-
makino
-
caulobacter
-
watanabe
- d-glucarate
-
tricarboxylic
- crescentus
- subtilis
-
3-hydroxypropionic
- d-xylose
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.26
-
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RECOMMENDED NAME
GeneOntology No.
2,5-dioxovalerate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2,5-dioxopentanoate:NADP+ 5-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY
37250-92-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
alpha-ketoglutaric semialdehyde + NADP+ + H2O
alpha-ketoglutarate + NADPH + H+
-
-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
-
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is specific for NADP+
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
-
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
the enzyme is specific for NADP+
-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
-
-
-
-
?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
the enzyme is specific for NADP+
-
-
?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
the enzyme is specific for NADP+
-
-
?
glutaraldehyde + NAD(P)+ + H2O
glutarate + NAD(P)H + H+
-
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
the enzyme is specific for NADP+
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
the enzyme is specific for NADP+
-
-
?
succinate semialdehyde + NAD(P)+ + H2O
? + NAD(P)H + H+
-
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
-
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
; no significant preference between NAD+ and NADP+ in activity; prefered cofactor of KGSADH-II
NADP+
alpha-KGSA dehydrogenase is an NADP+-preferring enzyme, since it is 58times more efficient with NADP+ than with NAD+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibitory effect with alpha-ketoglutarate or glutamate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.37
glycolaldehyde
-
pH 6.0, 70°C, native enzyme form xylose-grown cells
0.0065
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
0.0075
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
0.011
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
0.0246
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.4
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
21.3
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
23
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
53.9
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
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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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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
2 * 57000 or 2 * 54351, gel filtration; 2 * 57000 or 2 * 55185, gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
tetramer
dimer
2 * 57000 or 2 * 54351, gel filtration; 2 * 57000 or 2 * 55185, gel filtration
dimer
-
2 * 57000 or 2 * 54351, gel filtration; 2 * 57000 or 2 * 55185, gel filtration
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
KGSADH-III purified on nickel-nitrilotriacetic acid spin column and by gel filtration; KGSADH-II purified on nickel-nitrilotriacetic acid spin column and by gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
KGSADH-III overexpressed as His6-tagged protein in Escherichia coli DH5alpha; KGSADH-II overexpressed as His6-tagged protein in Escherichia coli DH5alpha
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
alpha-KGSA dehydrogenase activity in cell extracts from the mutant DELTAACIAD0131 grown on succinate as the sole carbon source is undetectable
additional information
-
alpha-KGSA dehydrogenase activity in cell extracts from the mutant DELTAACIAD0131 grown on succinate as the sole carbon source is undetectable
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
additional information
degradation
involved in an alternative pathway of D-glucarate metabolism
degradation
involved in an alternative pathway of D-glucarate metabolism
degradation
-
involved in an alternative pathway of D-glucarate metabolism
-
additional information
-
three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently
additional information
-
the ALDH branch including ycbD protein is designated the KGSADH subclass (type III)
additional information
-
three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently; three different types of KGSADH appear in the bacterial evolutional stage convergently
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.26)
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