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Information on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase and Organism(s) Mus musculus and UniProt Accession Q8CHT0

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EC Tree
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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This record set is specific for:
Mus musculus
UNIPROT: Q8CHT0
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The taxonomic range for the selected organisms is: Mus musculus
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, 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
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glyoxylate
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L-glutamate
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L-glutarate
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succinate
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additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.27
glyoxylate
pH 7.0, 20°C
12
L-glutamate
pH 7.0, 20°C
30
L-glutarate
pH 7.0, 20°C
58
succinate
pH 7.0, 20°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AL4A1_MOUSE
562
0
61841
Swiss-Prot
Mitochondrion (Reliability: 1)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with glutarate, succinate, malonate, glyoxylate, and acetate
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pemberton, T.A.; Tanner, J.J.
Structural basis of substrate selectivity of delta(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length
Arch. Biochem. Biophys.
538
34-40
2013
Mus musculus (Q8CHT0), Mus musculus
Manually annotated by BRENDA team