Pyrroline-5-carboxylate reductase explained
pyrroline-5-carboxylate reductase |
Ec Number: | 1.5.1.2 |
Cas Number: | 9029-17-8 |
Go Code: | 0004735 |
Width: | 270 |
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In enzymology, a pyrroline-5-carboxylate reductase 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,,,, and .
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 . 10.1016/S0021-9258(18)64497-7 . 13681369 . free .
- 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 . 10.1016/S0021-9258(19)63684-7 . 13502341. free .
- Smith ME . Greenberg DM . Characterization of an enzyme reducing pyrroline-5-carboxylate to proline . Nature. 1956 . 177. 4520. 1130 . 10.1038/1771130a0 . 13334497 . 1956Natur.177.1130S . 4298013 . free .
- 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 . 10.1016/S0021-9258(18)70299-8 . 13630905 . free .