Pyrroline-5-carboxylate reductase
ExPASy NiceZyme view | | ||||||||
| KEGG | KEGG entry | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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
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
.
Human genes
- PYCR1, nuclear gene for mitochondrial protein
- PYCR2, nuclear gene for mitochondrial protein
- PYCR3 (formerly PYCRL), cytosolic protein
References
- Adams E; Goldstone A (1960). "Hydroxyproline metabolism. III. Enzymatic synthesis of hydroxyproline from Delta1-pyrroline-3-hydroxy-5-carboxylate". The Journal of Biological Chemistry. 235 (12): 3499–3503. PMID 13681369.
- Meister A, Radhakrishnan AN, Buckley SD (1957). "Enzymatic synthesis of L-pipecolic acid and L-proline". The Journal of Biological Chemistry. 229 (2): 789–800. PMID 13502341.
- Smith ME; Greenberg DM (1956). "Characterization of an enzyme reducing pyrroline-5-carboxylate to proline". Nature. 177 (4520): 1130. S2CID 4298013.
- Yura T; Vogel HJ (1959). "Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties". The Journal of Biological Chemistry. 234 (2): 335–338. PMID 13630905.
