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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
- l-arabinose
-
azospirillum
- crescentus
-
3-hydroxypropionic
- d-xylose
-
tricarboxylic
- aldolase
- isozymes
-
caulobacter
-
watanabe
-
makino
- degradation
- d-glucarate
The enzyme appears in viruses and cellular organisms
Synonyms
2-oxoglutarate semialdehyde dehydrogenase, alpha-ketoglutarate semialdehyde dehydrogenase, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-KGSA dehydrogenase, alphaKGSA dehydrogenase, alphaKGSADH, DopDH, KGSADH, KGSADH-I, KGSADH-II, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoglutarate semialdehyde dehydrogenase
-
-
-
-
alpha-ketoglutarate semialdehyde dehydrogenase
alpha-ketoglutaric semialdehyde dehydrogenase
alpha-KGSA dehydrogenase
alphaKGSA dehydrogenase
alphaKGSADH
DopDH
KGSADH-I
KGSADH-II
KGSADH-III
SSO3117
alpha-ketoglutaric semialdehyde dehydrogenase
-
-
-
-
alpha-ketoglutaric semialdehyde dehydrogenase
-
alpha-ketoglutaric semialdehyde 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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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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
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 + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
r
2,5-dioxopentanoate + NAD+ + H2O
2-oxoglutarate + NADH + H+
-
-
-
r
2,5-dioxopentanoate + NADP+ + H2O
2-oxoglutarate + NADPH + 2 H+
-
-
-
?
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 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
-
-
?
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+
-
-
-
?
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+
-
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + 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+
-
-
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
-
-
-
?
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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
2,5-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
NAD+
no significant preference between NAD+ and NADP+ in activity
NADP+
alpha-KGSA dehydrogenase is an NADP+-preferring enzyme, since it is 58times more efficient with NADP+ than with NAD+
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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
0.0246
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.3
alpha-Ketoglutaric semialdehyde
with NAD+ as cofactor
15.4
alpha-Ketoglutaric semialdehyde
with NADP+ as cofactor
23
alpha-Ketoglutaric semialdehyde
with NADP+ 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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (1010 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
57000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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-II purified on nickel-nitrilotriacetic acid spin column and by gel filtration
KGSADH-III 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-II overexpressed as His6-tagged protein in Escherichia coli DH5alpha
KGSADH-III overexpressed as His6-tagged protein in Escherichia coli DH5alpha
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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
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
additional information
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
additional information
-
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
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schimz, K.L.; Kurz, G.
Regulation of L-arabinose metabolism in Pseudomonas fluorescens
Biochem. Soc. Trans.
3
1087-1089
1975
Pseudomonas fluorescens
-
brenda
Dilworth, M.J.; Arwas, R.; McKay, I.A.; Saroso, S.; Glenn, A.R.
Pentose metabolism in Rhizobium leguminosarum MNF300 and in cowpea Rhizobium NGR234
J. Gen. Microbiol.
132
2733-2742
1986
Bradyrhizobium japonicum, Bradyrhizobium sp., Rhizobium leguminosarum, Rhizobium sp., Sinorhizobium meliloti
-
brenda
Adams, E.; Rosso, G.
alpha-Ketoglutaric semialdehyde dehydrogenase of Pseudomonas. Properties of the purified enzyme induced by hydroxyproline and of the glucarate-induced and constitutive enzymes
J. Biol. Chem.
242
1802-1814
1967
Pseudomonas sp.
brenda
Watanabe, S.; Yamada, M.; Ohtsu, I.; Makino, K.
alpha-ketoglutaric semialdehyde dehydrogenase isozymes involved in metabolic pathways of D-glucarate, D-galactarate, and hydroxy-L-proline. Molecular and metabolic convergent evolution
J. Biol. Chem.
282
6685-6695
2007
Azospirillum brasilense (Q08IB7), Azospirillum brasilense (Q08IC0), Azospirillum brasilense (Q1JUP4), Azospirillum brasilense, Azospirillum brasilense ATCC 29145 (Q08IB7), Azospirillum brasilense ATCC 29145 (Q08IC0), Azospirillum brasilense ATCC 29145 (Q1JUP4), Bacillus subtilis
brenda
Aghaie, A.; Lechaplais, C.; Sirven, P.; Tricot, S.; Besnard-Gonnet, M.; Muselet, D.; de Berardinis, V.; Kreimeyer, A.; Gyapay, G.; Salanoubat, M.; Perret, A.
New Insights into the Alternative D-Glucarate Degradation Pathway
J. Biol. Chem.
283
15638-15646
2008
Acinetobacter baylyi (Q6FFQ0), Pseudomonas putida (Q88GW5)
brenda
Nunn, C.E.; Johnsen, U.; Schoenheit, P.; Fuhrer, T.; Sauer, U.; Hough, D.W.; Danson, M.J.
Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius
J. Biol. Chem.
285
33701-33709
2010
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
brenda
Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment
J. Biol. Chem.
281
27378-27388
2006
Saccharolobus solfataricus (Q97UA1), Saccharolobus solfataricus P2 (Q97UA1)
brenda
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