Proline dehydrogenase

Proline dehydrogenase

In enzymology, a proline dehydrogenase is an enzyme that catalyzes the chemical reaction

L-proline + acceptor rightleftharpoons (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.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .


  • Scarpulla RC, Soffer RL "Membrane-bound proline dehydrogenase from Escherichia coli Solubilization, purification, and characterization". J. Biol. Chem. 253 5997–6001.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes

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