EC 1.5.5.2 - Proline dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.5.5.2

Names

Accepted name:
proline dehydrogenase
Other names:
L-proline dehydrogenase
L-proline:(acceptor) oxidoreductase
Systematic name:
L-proline:quinone oxidoreductase

Reactions

Cofactor

Comments:

A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor [3]. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00068
Structural data: CSA , EC2PDB
CAS Registry Number: 9050-70-8
UniProtKB/Swiss-Prot: (26) [show] [UniProt]

References

  1. Scarpulla, R.C. and Sofer, R.L.
    Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization.
    J. Biol. Chem. 253: 5997-6001 (1978). [PMID: 355248]
  2. Brown, E.D. and Wood, J.M.
    Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.
    J. Biol. Chem. 267: 13086-13092 (1992). [PMID: 1618807]
  3. Moxley, M. A., Tanner, J. J., Becker, D. F.
    Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli.
    Arch. Biochem. Biophys. 516: 113-120 (2011). [PMID: 22040654]

[EC 1.5.5.2 created 1980 as EC 1.5.99.8, modified 2008, transferred 2013 to EC 1.5.5.2]