Pyrroline-5-carboxylate reductase
| pyrroline-5-carboxylate reductase | |||||||||
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Pyrroline-5-carboxylate reductase dekamer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 1.5.1.2 | ||||||||
| CAS number | 9029-17-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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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
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2AHR, 2GER, 2GR9, 2GRA, and 2IZZ.
References
- 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.