Biology:1-Pyrroline-5-carboxylate dehydrogenase

From HandWiki
Short description: Class of enzymes
1-pyrroline-5-carboxylate dehydrogenase
Identifiers
EC number1.2.1.88
CAS number9054-82-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a 1-pyrroline-5-carboxylate dehydrogenase (EC 1.2.1.88) is an enzyme that catalyzes the chemical reaction

(S)-1-pyrroline-5-carboxylate + NAD+ + 2 H2O [math]\displaystyle{ \rightleftharpoons }[/math] L-glutamate + NADH + H+

The three substrates of this enzyme are (S)-1-pyrroline-5-carboxylate, NAD+, and H2O, whereas its three products are glutamate, NADH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-1-pyrroline-5-carboxylate:NAD+ oxidoreductase. Other names in common use include delta-1-pyrroline-5-carboxylate dehydrogenase, 1-pyrroline dehydrogenase, pyrroline-5-carboxylate dehydrogenase, pyrroline-5-carboxylic acid dehydrogenase, L-pyrroline-5-carboxylate-NAD+ oxidoreductase, and 1-pyrroline-5-carboxylate:NAD+ oxidoreductase. This enzyme participates in glutamate metabolism and arginine and proline metabolism.

Structural studies

As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 2BHP, 2BHQ, 2BJA, 2BJK, 2EHQ, 2EHU, 2EII, 2EIT, 2EIW, 2EJ6, 2EJD, 2EJL, 2IY6, and 2J40.

Human gene

In human, the protein is encoded by ALDH4A1 gene.

References

  • "Hydroxyproline metabolism. IV. Enzymatic synthesis of gamma-hydroxyglutamate from Delta 1-pyrroline-3-hydroxy-5-carboxylate". The Journal of Biological Chemistry 235 (12): 3504–12. December 1960. doi:10.1016/S0021-9258(18)64498-9. PMID 13681370. 
  • "The interconversion of glutamic acid proline. III Delta1-Pyrroline-5-carboxylic acid dehydrogenase". J. Biol. Chem. 235: 3218–3223. 1960. doi:10.1016/S0021-9258(20)81340-4.