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Information on EC 1.2.1.26 - 2,5-dioxovalerate dehydrogenase
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EC Tree
1.2.1.26 2,5-dioxovalerate dehydrogenaseSpecify your search results
Word Map
- 1.2.1.26
- dehydratase
-
azospirillum
-
aldhs
-
3-hydroxypropionic
- brasilense
- l-arabinose
- aldolase
- d-glucarate
-
watanabe
- crescentus
-
tricarboxylic
-
makino
- d-xylose
- degradation
- isozymes
-
caulobacter
The enzyme appears in viruses and cellular organisms
Synonyms
kgsadh, kgsadh-iii, kgsadh-ii, alpha-ketoglutaric semialdehyde dehydrogenase, abkgsadh, alpha-ketoglutarate semialdehyde dehydrogenase, kgsadh-i, ycbd protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoglutarate semialdehyde dehydrogenase
-
-
-
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alpha-ketoglutarate semialdehyde dehydrogenase
alpha-ketoglutaric semialdehyde dehydrogenase
alpha-KGSA dehydrogenase
alphaKGSA dehydrogenase
alphaKGSADH
DopDH
KGSADH
KGSADH-I
KGSADH-II
KGSADH-III
SSO3117
additional information
alpha-ketoglutaric semialdehyde dehydrogenase
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-
-
-
alpha-ketoglutaric semialdehyde dehydrogenase
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alpha-ketoglutaric semialdehyde dehydrogenase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + H+
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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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-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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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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-oxoglutaric semialdehyde + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + H+
-
-
-
?
2-oxoglutaric semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
?
3-hydroxypropionaldehyde + NADP+
3-hydroxypropionate + NADPH + H+
very low activity
-
-
?
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
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-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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-
-
?
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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-
-
r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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-
-
r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
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-
-
r
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
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-
?
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+
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
-
-
?
3-hydroxypropionaldehyde + NAD+
3-hydroxypropionate + NADH + H+
-
-
-
?
3-hydroxypropionaldehyde + NAD+
3-hydroxypropionate + NADH + H+
-
-
-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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-
-
?
alpha-ketoglutaric semialdehyde + NAD(P)+ + H2O
alpha-ketoglutarate + NAD(P)H + H+
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-
-
-
?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
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-
-
?
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+
-
-
?
DL-glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
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-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
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-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
the enzyme is specific for NADP+
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
the enzyme is specific for NADP+
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
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-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
activity of EC 1.2.1.24
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-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
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activity of EC 1.2.1.24
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-
?
additional information
?
-
substrate and cofactor binding structures analysis, overview. The enzyme shows poor activity with NADP+ as a cofactor
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-
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additional information
?
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substrate and cofactor binding structures analysis, overview. The enzyme shows poor activity with NADP+ as a cofactor
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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-oxoglutaric semialdehyde + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + H+
-
-
-
?
2-oxoglutaric semialdehyde + NAD+ + H2O
2-oxoglutarate + NADH + H+
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-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
-
-
-
?
2,5-dioxopentanoate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H
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-
-
?
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
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
activity of EC 1.2.1.24
-
-
?
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
-
activity of EC 1.2.1.24
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
no significant preference between NAD+ and NADP+ in activity
NAD+
NAD+-enzyme binding mode and structure, overview. The NAD+-binding pocket is constituted by seven loops (beta7-alpha4, beta8-alpha5, beta10-alpha7, beta11-beta12, alpha8-beta13, alpha9-alpha10, and alpha11-beta16) and four alpha-helices (alpha4, alpha6, alpha7, and alpha10). The adenine ring is stabilized in the hydrophobic pocket that is formed by Phe151, Pro211, Ala212, Phe229, Val235 and Leu239, and a hydrogen bond with Ser215 also contributes to the binding of the ring. Residues Lys178, Glu181, and Pro211 constitute a suitable space for binding of the ribose ring, and stabilize the 2'-hydroxyl-group of the ring. The formation of the ribose ring binding site does not seem to be large enough to accommodate the phosphorylated ribose ring. Therefore the enzyme shows poor activity with NADP+ as a cofactor. The diphosphate moiety is stabilized by residues Asn331, Arg333, and Arg334 through directly and water-mediated hydrogen bond networks. Residues Arg334 and Glu384 stabilize the ribose moiety of NAD+, and the nicotinamide ring is stabilized by residues Gln160 and Glu253 by hydrogen bonding
NAD+
preferred cofactor, residues chosen for generating the NAD+ binding pocket library are shown using the crystal structure of KGSADH complexed with NAD+ (PDB ID 5X5U), overview
NADP+
alpha-KGSA dehydrogenase is an NADP+-preferring enzyme, since it is 58times more efficient with NADP+ than with NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
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
0.17
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
0.29
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.43
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
0.55
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R
0.78
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
1.4
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A442P/P444T
1.6
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant wild-type enzyme
2.2
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
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
0.025
NAD+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.033
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
0.037
NAD+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
0.27
NAD+
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
0.28
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
0.54
NADP+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
0.66
NADP+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
0.7
NADP+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
6
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
6.7
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
6.8
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant R334Q/A337R
11
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A
12
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A442P/P444T
15
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant wild-type enzyme
15
3-hydroxypropionaldehyde
pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T
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
4.8
NAD+
pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T
5.9
NAD+
pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T
6.1
NAD+
pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A
12
NAD+