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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 .
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,
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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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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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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
additional information
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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 involved in L-proline catabolism
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additional information
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slight activity with glutaric semialdehyde and adipic semialdehyde
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1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
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ir
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Atherosclerosis
ALDH4A1 is an atherosclerosis auto-antigen targeted by protective antibodies.
Cataract
Investigation of eight candidate genes on chromosome 1p36 for autosomal dominant total congenital cataract.
Epilepsy
Metabolic epilepsy in hyperprolinemia type II due to a novel nonsense ALDH4A1 gene variant.
Fascioliasis
Proline in fascioliasis: III. Activities of pyrroline-5-carboxylic acid reductase and pyrroline-5-carboxylic acid dehydrogenase in Fasciola.
Granuloma
Proline trapping in granulomas, the site of collagen biosynthesis in murine schistosomiasis.
Hypersensitivity
The role of [Delta]1-pyrroline-5-carboxylate dehydrogenase in proline degradation.
Infections
P5CDH affects the pathways contributing to Pro synthesis after ProDH activation by biotic and abiotic stress conditions.
Infections
Proteomic comparison of Mycobacterium avium subspecies paratuberculosis grown in vitro and isolated from clinical cases of ovine paratuberculosis.
Infections
Reactive oxygen species homeostasis and virulence of the fungal pathogen Cryptococcus neoformans requires an intact proline catabolism pathway.
l-glutamate gamma-semialdehyde dehydrogenase deficiency
Crystal Structure of Thermus thermophilus Delta(1)-Pyrroline-5-carboxylate Dehydrogenase.
Metabolic Diseases
Polymorphisms of human aldehyde dehydrogenases. Consequences for drug metabolism and disease.
Metabolic Syndrome
In Vivo Exposures to Particulate Matter Collected from Saudi Arabia or Nickel Chloride Display Similar Dysregulation of Metabolic Syndrome Genes.
Neoplasms
Aldehyde dehydrogenases and cell proliferation.
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0.17
1-pyrroline-5-carboxylate
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SwissProt
brenda
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northern blot analysis
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northern blot analysis
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northern blot analysis
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northern blot analysis
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northern blot analysis
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matrix
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matrix
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AL4A1_HUMAN
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61719
Swiss-Prot
Mitochondrion (Reliability: 1 )
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62000
? * 62000, DNA sequence determination
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? * 62000, DNA sequence determination
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the substrate-free form displays multiple active site conformations. Protein forms a trimer-of-dimers hexamer in solution
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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
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expression in Escherichia coli
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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.
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18668-18672
1990
Homo sapiens, Rattus norvegicus
brenda
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
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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
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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
brenda
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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