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Information on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P09546
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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 taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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, gsaldh, delta1-pyrroline-5-carboxylate dehydrogenase, delta1-pyrroline-5-carboxylate synthetase, pyrroline-5-carboxylic acid dehydrogenase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
proline/P5C dehydrogenase
bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
PutA
1-pyrroline dehydrogenase
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dehydrogenase, 1-pyrroline-5-carboxylate
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DELTA1-pyrroline-5-carboxylate dehydrogenase
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L-pyrroline-5-carboxylate-NAD+ oxidoreductase
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pyrroline-5-carboxylate dehydrogenase
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pyrroline-5-carboxylic acid dehydrogenase
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PutA
bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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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].
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 + NAD+ + H2O
L-glutamate + NADH + H+
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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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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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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
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
25°C, pH 7.5, pH 7.5, L-glutamate gamma-semialdehyde dehydrogenase activity proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase, reactions of EC 1.5.5.2 and 1.2.1.88, respectively
UniProt
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
137000
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE
293000
gel filtration, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, sucrose density centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brown, E.D.; Wood, J.M.
Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli
J. Biol. Chem.
267
13086-13092
1992
Escherichia coli (P09546), Escherichia coli
Moxley, M.A.; Sanyal, N.; Krishnan, N.; Tanner, J.J.; Becker, D.F.
Evidence for hysteretic substrate channeling in the proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA)
J. Biol. Chem.
289
3639-3651
2014
Escherichia coli (P09546), Escherichia coli
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