Proline dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a proline dehydrogenase (EC 1.5.99.8) is an enzyme that catalyzes the chemical reaction
- L-proline + acceptor
(S)-1-pyrroline-5-carboxylate + reduced acceptor
Thus, the two substrates of this enzyme are L-proline and acceptor, whereas its two products are (S)-1-pyrroline-5-carboxylate and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with other acceptors. The systematic name of this enzyme class is L-proline:acceptor oxidoreductase. Other names in common use include L-proline dehydrogenase, and L-proline:(acceptor) oxidoreductase. This enzyme participates in arginine and proline metabolism. It employs one cofactor, FAD.
Contents |
[edit] Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1K87, 1TIW, 1TJ0, 1TJ1, 1TJ2, 1Y56, 2FZM, 2FZN, and 2G37.
[edit] References
- IUBMB entry for 1.5.99.8
- BRENDA references for 1.5.99.8 (Recommended.)
- PubMed references for 1.5.99.8
- PubMed Central references for 1.5.99.8
- Google Scholar references for 1.5.99.8
- Scarpulla RC, Soffer RL (1978). "Membrane-bound proline dehydrogenase from Escherichia coli Solubilization, purification, and characterization". J. Biol. Chem. 253: 5997–6001. PMID 355248.
[edit] External links
-
- The CAS registry number for this enzyme class is 9050-70-8.
[edit] Gene Ontology (GO) codes
 |
This EC 1.5 enzyme-related article is a stub. You can help Wikipedia by expanding it. |
