Pyrroline-5-carboxylate reductase

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pyrroline-5-carboxylate reductase
2izz.jpg
Pyrroline-5-carboxylate reductase 1 dekamer, Human
Identifiers
EC number1.5.1.2
CAS number9029-17-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a pyrroline-5-carboxylate reductase (EC 1.5.1.2) is an enzyme that catalyzes the chemical reaction

L-proline + NAD(P)+ 1-pyrroline-5-carboxylate + NAD(P)H + H+

The 3 substrates of this enzyme are L-proline, NAD+, and NADP+, whereas its 4 products are 1-pyrroline-5-carboxylate, NADH, NADPH, 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 L-proline:NAD(P)+ 5-oxidoreductase. Other names in common use include proline oxidase, L-proline oxidase, 1-pyrroline-5-carboxylate reductase, NADPH-L-Delta1-pyrroline carboxylic acid reductase, and L-proline-NAD(P)+ 5-oxidoreductase. This enzyme participates in arginine and proline metabolism.

Structural studies[edit]

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2AHR, 2GER, 2GR9, 2GRA, and 2IZZ.

Human genes[edit]

  • PYCR1, nuclear gene for mitochondrial protein
  • PYCR2, nuclear gene for mitochondrial protein
  • PYCR3 (formerly PYCRL), cytosolic protein

References[edit]

  • Adams E; Goldstone A (1960). "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate". J. Biol. Chem. 235: 3499–3503.
  • Meister A, Radhakrishnan AN, Buckley SD (1957). "Enzymatic synthesis of L-pipecolic acid and L-proline". J. Biol. Chem. 229 (2): 789–800. PMID 13502341.
  • Smith ME; Greenberg DM. "Characterization of an enzyme reducing pyrroline-5-carboxylate to proline". N. Lond. Nature: 1130.
  • Yura T; Vogel HJ (1959). "Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties". J. Biol. Chem. 234: 335–338.