1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase
This is an abbreviated version!
For detailed information about L-glutamate gamma-semialdehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.88
Reaction
Synonyms
1-pyrroline dehydrogenase, aldehyde dehydrogenase 12, ALDH12, Aldh4a1, dehydrogenase, 1-pyrroline-5-carboxylate, DELTA1-pyrroline-5-carboxylate dehydrogenase, delta1-pyrroline-5-carboxylate synthetase, DR_0813, EC 1.5.1.12, GSAL dehydrogenase, GSALDH, l-glutamate-gamma-semialdehyde dehydrogenase, L-pyrroline-5-carboxylate-NAD+ oxidoreductase, LRRP Ba1-651, NAD+-dependent glutamate gamma-semialdehyde dehydrogenase, OsALDH12, OsALDH18-2, P5C dehydrogenase, P5C synthase, P5C-DH, P5CD, P5CDH, P5CDH1, P5CS, PDH, PpALDH12, proline/P5C dehydrogenase, Put2, PutA, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylate synthase, pyrroline-5-carboxylic acid dehydrogenase, Tc00.1047053510943.50, YcgN, ZmALDH12
ECTree
1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase
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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
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
-
-
-
?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
-
as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
-
as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
-
as active as 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
41% activity compared to 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
2fold higher activity than with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
D-glucose + NAD+ + H2O
D-gluconate + NADH
-
80% of the activity with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
formaldehyde + NAD+ + H2O
formate + NADH
-
50% of activity with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
glyceralaldehyde-3-phosphate + NAD+ + H2O
glycerate-3-phosphate + NADH
-
slight activity with isoforms A and B
-
-
?
glyoxylic acid + NAD+ + H2O
oxalic acid + NADH
-
41% activity of that with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
66% activity of that with 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
indole-3-phosphate + NAD+ + H2O
?
-
slight activity with isoforms A and B
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
highly specific
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
-
ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
-
r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
-
NAD+ is preferred over NADP+
-
-
ir
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
about 6% activity compared to L-glutamate 5-semialdehyde
-
-
?
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
about 6% activity compared to L-glutamate 5-semialdehyde
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
about 7.5% activity compared to L-glutamate 5-semialdehyde
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
about 7.5% activity compared to L-glutamate 5-semialdehyde
-
-
?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
-
-
-
?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
-
-
-
-
?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
two-electron oxidation in which a hydride is transferred toNAD+, producing NADH and glutamate
-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
-
-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
NAD+ is the preferred cofactor
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
NAD+ is the preferred cofactor
-
-
ir
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
ir
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
?
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
?
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
-
-
-
ir
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
about 2% activity compared to L-glutamate 5-semialdehyde
-
-
?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
about 2% activity compared to L-glutamate 5-semialdehyde
-
-
?
additional information
?
-
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
-
-
?
additional information
?
-
-
kinetic model for the overall PRODH-P5CDH reaction of bifunctional PutA enzyme. The intermediate is not released into the bulk medium, but the mechanism follows substrate channeling. The rate of NADH formation is 20fold slower than the steady-state turnover number for the overall reaction, The limiting rate constant observed for NADH formation in the first turnover increases by almost 40fold after multiple turnovers, achieving half of the steady-state value after 15 turnovers
-
-
?
additional information
?
-
-
slight activity with glutaric semialdehyde and adipic semialdehyde
-
-
?
additional information
?
-
-
additional esterase activity with p-nitrophenyl acetate as substrate, 50% of activity with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
additional information
?
-
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
Q0DHN6
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
additional information
?
-
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
additional information
?
-
-
slight activity with glutaric semialdehyde and adipic semialdehyde
-
-
?
additional information
?
-
-
enzyme involved in L-proline catabolism
-
-
?
additional information
?
-
-
enzyme with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase, which require different reaction conditions
-
-
?
additional information
?
-
-
enzyme with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase, which require different reaction conditions
-
-
?
additional information
?
-
-
catalyzes last step in both arginine and proline catabolism
-
-
?
additional information
?
-
-
no reverse reaction using L-glutamate as substrate within pH 5.5 to pH 10.0
-
-
?
additional information
?
-
the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
-
-
-
