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Information on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase
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1.2.1.88 L-glutamate gamma-semialdehyde dehydrogenaseIUBMB Comments
This enzyme catalyses the irreversible oxidation of glutamate-gamma-semialdehyde to glutamate as part of the proline degradation pathway. (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. NADP+ can also act as acceptor, but with lower activity .
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
p5cdh, aldh4a1, p5c dehydrogenase, 1-pyrroline-5-carboxylate dehydrogenase, p5c synthase, pyrroline-5-carboxylate dehydrogenase, delta1-pyrroline-5-carboxylate dehydrogenase, gsaldh, delta1-pyrroline-5-carboxylate synthetase, pyrroline-5-carboxylic acid dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-pyrroline dehydrogenase
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aldehyde dehydrogenase 12
ALDH12
Aldh4a1
dehydrogenase, 1-pyrroline-5-carboxylate
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DELTA1-pyrroline-5-carboxylate dehydrogenase
DR_0813
EC 1.5.1.12
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formerly
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GSAL dehydrogenase
GSALDH
l-glutamate-gamma-semialdehyde dehydrogenase
L-pyrroline-5-carboxylate-NAD+ oxidoreductase
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NAD+-dependent glutamate gamma-semialdehyde dehydrogenase
P5C dehydrogenase
P5CDH
P5CDH1
proline/P5C dehydrogenase
bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
PutA
pyrroline-5-carboxylate dehydrogenase
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pyrroline-5-carboxylic acid dehydrogenase
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Tc00.1047053510943.50
DELTA1-pyrroline-5-carboxylate dehydrogenase
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PutA
bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
PutA
proline utilization A protein, bifunctional proline catabolic enzyme that catalyzes the 4-electron oxidation of L-proline to L-glutamate using spatially-separated proline dehydrogenase and L-glutamate-gamma-semialdehyde dehydrogenase active sites
PutA
proline utilization A protein, bifunctional proline catabolic enzyme that catalyzes the 4-electron oxidation of L-proline to L-glutamate using spatially-separated proline dehydrogenase and L-glutamate-gamma-semialdehyde dehydrogenase active sites
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
no induction by ammonia
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
induction by proline, activation on gene transcription level
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
ordered reaction mechanism
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
enzyme is a gamma-glutamyl semialdehyde dehydrogenase
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
induction by proline
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
induction by proline
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L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
induction by proline, activation on gene transcription level
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
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oxidation
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate gamma-semialdehyde:NAD+ oxidoreductase
This enzyme catalyses the irreversible oxidation of glutamate-gamma-semialdehyde to glutamate as part of the proline degradation pathway. (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. NADP+ can also act as acceptor, but with lower activity [5].
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CAS REGISTRY NUMBER
COMMENTARY
9054-82-4
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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+
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?
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
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as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
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?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
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as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
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?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
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as active as 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
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?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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41% activity compared to 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
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?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
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2fold higher activity than with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
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?
D-glucose + NAD+ + H2O
D-gluconate + NADH
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80% of the activity with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
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?
formaldehyde + NAD+ + H2O
formate + NADH
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50% of activity with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
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?
glyceralaldehyde-3-phosphate + NAD+ + H2O
glycerate-3-phosphate + NADH
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slight activity with isoforms A and B
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?
glyoxylic acid + NAD+ + H2O
oxalic acid + NADH
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41% activity of that with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
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?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
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66% activity of that with 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
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?
indole-3-phosphate + NAD+ + H2O
?
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slight activity with isoforms A and B
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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highly specific
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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-
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
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r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
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r
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
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?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
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r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
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r
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
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NAD+ is preferred over NADP+
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ir
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
about 6% activity compared to L-glutamate 5-semialdehyde
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?
2-aminoadipic semialdehyde + NAD+ + H2O
2-aminoadipate + NADH + H+
about 6% activity compared to L-glutamate 5-semialdehyde
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?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
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?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
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?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
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?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
about 7.5% activity compared to L-glutamate 5-semialdehyde
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?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
about 7.5% activity compared to L-glutamate 5-semialdehyde
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?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
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?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
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?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH + H+
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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two-electron oxidation in which a hydride is transferred toNAD+, producing NADH and glutamate
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?
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+
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?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
NAD+ is the preferred cofactor
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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-
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
NAD+ is the preferred cofactor
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ir
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
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ir
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
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?
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
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?
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
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ir
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
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?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
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?
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
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?
phenylpropionaldehyde + NAD+ + H2O
phenylpropionate + NADH + H+
about 5% activity compared to L-glutamate 5-semialdehyde
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?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
about 2% activity compared to L-glutamate 5-semialdehyde
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?
succinic semialdehyde + NAD+ + H2O
succinate + NADH + H+
about 2% activity compared to L-glutamate 5-semialdehyde
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?
additional information
?
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enzyme involved in L-proline catabolism
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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slight activity with glutaric semialdehyde and adipic semialdehyde
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?
additional information
?
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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
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?
additional information
?
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ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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?
additional information
?
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Q0DHN6
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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?
additional information
?
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the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
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additional information
?
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the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
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additional information
?
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slight activity with glutaric semialdehyde and adipic semialdehyde
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?
additional information
?
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enzyme involved in L-proline catabolism
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?
additional information
?
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enzyme with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase, which require different reaction conditions
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?
additional information
?
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enzyme with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase, which require different reaction conditions
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?
additional information
?
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catalyzes last step in both arginine and proline catabolism
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?
additional information
?
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no reverse reaction using L-glutamate as substrate within pH 5.5 to pH 10.0
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?
additional information
?
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the enzyme shows a narrow substrate preference for L-glutamate 5-semialdehyde (GSAL) and glutaric semialdehyde (GRSAL)
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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
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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-
-
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?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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-
-
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?
glutaric semialdehyde + NAD+ + H2O
glutarate + NADH + H+
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-
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ir
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+
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?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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-
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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ir
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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-
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ir
additional information
?
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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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the apparent catalytic efficiency for NAD+ is about 60fold higher than for NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information