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Information on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase and Organism(s) Homo sapiens and UniProt Accession P30038

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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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Homo sapiens
UNIPROT: P30038
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The taxonomic range for the selected organisms is: Homo sapiens
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
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
show the reaction diagram
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ir
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
show the reaction diagram
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ir
additional information
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NATURAL SUBSTRATE
NATURAL 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 + NAD+ + H2O
L-glutamate + NADH
show the reaction diagram
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ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
dependent on
NAD+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
1-pyrroline-5-carboxylate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
northern blot analysis
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AL4A1_HUMAN
563
0
61719
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
? * 62000, DNA sequence determination
142000
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gel filtration
66000
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66000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
? * 62000, DNA sequence determination
dimer
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66000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the substrate-free form displays multiple active site conformations. Protein forms a trimer-of-dimers hexamer in solution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E314A
inactive. The conserved Glu447 residue has significantly shifted in the mutant, causing NAD+ to be displaced
S352A
catalytic site including the oxoanion hole and residue Cys348 remain unchanged in the mutant, and the coenzyme maintains its binding position
S352L
inactive. The conserved Glu447 residue has significantly shifted in the mutant, causing NAD+ to be displaced
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Small, W.C.; Jones, M.E.
Pyrroline 5-carboxylate dehydrogenase of the mitochondrial matrix of rat liver. Purification, physical and kinetic characteristics
J. Biol. Chem.
265
18668-18672
1990
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Hu, C.A.; Lin, W.W.; Valle, D.
Cloning characterization, and expression of cDNAs encoding human DELTA1-pyrroline-5-carboxylate dehydrogenase
J. Biol. Chem.
271
9795-9800
1996
Homo sapiens (P30038), Homo sapiens
Manually annotated by BRENDA team
Donald, S.P.; Sun, X.Y.; Hu, C.A.A.; Yu, J.; Mei, J.M.; Valle, D.; Phang, J.M.
Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species
Cancer Res.
61
1810-1815
2001
Homo sapiens
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
Ion, B.; Aboelnga, M.; Gauld, J.
Insights from molecular dynamics on substrate binding and effects of active site mutations in delta1-pyrroline-5-carboxylate dehydrogenase
Can. J. Chem.
94
1151-1162
2016
Homo sapiens (P30038)
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Manually annotated by BRENDA team