Proline dehydrogenase

In enzymology, a proline dehydrogenase (EC 1.5.5.2, formerly EC 1.5.99.8) is an enzyme that catalyzes the chemical reaction

L-proline + ubiquinone (S)-1-pyrroline-5-carboxylate + ubiquinol
proline dehydrogenase
Proline dehydrogenase tetramer, Bradyrhizobium diazoefficiens
Identifiers
EC number1.5.5.2
CAS number9050-70-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are L-proline and ubiquinone, whereas its two products are (S)-1-pyrroline-5-carboxylate and ubiquinol.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a quinone or similar compounds as acceptors. The systematic name of this enzyme class is L-proline:quinone 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 1K87, 1TIW, 1TJ0, 1TJ1, 1TJ2, 1Y56, 2FZM, 2FZN, and 2G37.

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References
    • Scarpulla RC, Soffer RL (1978). "Membrane-bound proline dehydrogenase from Escherichia coli Solubilization, purification, and characterization". J. Biol. Chem. 253 (17): 5997–6001. PMID 355248.


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