EC - L-glutamate γ-semialdehyde dehydrogenase

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IntEnz Enzyme Nomenclature


Accepted name:
L-glutamate γ-semialdehyde dehydrogenase
Other names:
1-pyrroline dehydrogenase
Δ1-pyrroline-5-carboxylate dehydrogenase
L-pyrroline-5-carboxylate-NAD+ oxidoreductase
pyrroline-5-carboxylate dehydrogenase
pyrroline-5-carboxylic acid dehydrogenase
Δ1-pyrroline-5-carboxylic acid dehydrogenase
1-pyrroline-5-carboxylate:NAD+ oxidoreductase
1-pyrroline-5-carboxylate dehydrogenase
Systematic name:
L-glutamate γ-semialdehyde:NAD+ oxidoreductase



This enzyme catalyses the irreversible oxidation of glutamate-γ-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, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate γ-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].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00068
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003842
CAS Registry Number: 9054-82-4
UniProtKB/Swiss-Prot: (63) [show] [UniProt]


  1. Adams, E. and Goldstone, A.
    Hydroxyproline metabolism. IV. Enzymatic synthesis of γ-hydroxyglutamate from Δ1-pyrroline-3-hydroxy-5-carboxylate.
    J. Biol. Chem. 235 : 3504-3512 (1960). [PMID: 13681370]
  2. Strecker, H.J.
    The interconversion of glutamic acid and proline. III. Δ1-Pyrroline-5-carboxylic acid dehydrogenase.
    J. Biol. Chem. 235 : 3218-3223 (1960).
  3. Forlani, G., Scainelli, D. and Nielsen, E.
    Δ1-Pyrroline-5-carboxylate dehydrogenase from cultured cells of potato. Purification and Properties.
    Plant Physiol. 113 : 1413-1418 (1997). [PMID: 12223682]
  4. Brown, E.D. and Wood, J.M.
    Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.
    J. Biol. Chem. 267 : 13086-13092 (1992). [PMID: 1618807]
  5. Inagaki, E., Ohshima, N., Sakamoto, K., Babayeva, N.D., Kato, H., Yokoyama, S. and Tahirov, T.H.
    New insights into the binding mode of coenzymes: structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+.
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 : 462-465 (2007). [PMID: 17554163]

[EC created 1972 as, modified 2008, transferred 2013 to EC]