Proline dehydrogenase

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proline dehydrogenase
4q72.jpg
Proline dehydrogenase tetramer, Bradyrhizobium diazoefficiens
Identifiers
EC number 1.5.5.2
CAS number 9050-70-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

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

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[edit]

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.

References[edit]

  • 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.