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Information on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07275

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IUBMB 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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Saccharomyces cerevisiae
UNIPROT: P07275
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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, pyrroline-5-carboxylic acid dehydrogenase, delta1-pyrroline-5-carboxylate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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 hide
9054-82-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
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?
additional information
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enzyme involved in L-proline catabolism
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.104
1-pyrroline-5-carboxylate
pH 7.5, 20°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
1-pyrroline-5-carboxylate
pH 7.5, 20°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
1-pyrroline-5-carboxylate
pH 7.5, 20°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.124
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wild-type
additional information
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activity depends on the nitrogen source for cell growth
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with NAD+, to 1.95 and 2.17 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W193A
mutation disrupts hexamer formation, mutant forms a dimer
additional information
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mutant strain MB2281-10C with deficiency in enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brandriss, M.C.; Magasanik, B.
Proline: an essential intermediate in arginine degradation in Saccharomyces cerevisiae
J. Bacteriol.
143
1403-1410
1980
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Brandriss, M.C.
Proline utilization in Saccharomyces cerevisiae: analysis of the cloned PUT2 gene
Mol. Cell. Biol.
3
1846-1856
1983
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Pemberton, T.A.; Srivastava, D.; Sanyal, N.; Henzl, M.T.; Becker, D.F.; Tanner, J.J.
Structural studies of yeast delta(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state
Biochemistry
53
1350-1359
2014
Homo sapiens (P30038), Homo sapiens, Saccharomyces cerevisiae (P07275), Saccharomyces cerevisiae
Manually annotated by BRENDA team