| EC |
1.5.5.2 |
| Accepted name: |
proline dehydrogenase |
| Reaction: |
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol |
| Other name(s): |
L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase |
| Systematic name: |
L-proline:quinone oxidoreductase |
| 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: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9050-70-8 |
| References: |
| 1. |
Scarpulla, R.C. and Sofer, R.L. Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. J. Biol. Chem. 253 (1978) 5997–6001. [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 (1992) 13086–13092. [PMID: 1618807] |
| 3. |
Moxley, M.A., Tanner, J.J. and 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 (2011) 113–120. [DOI] [PMID: 22040654] |
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| [EC 1.5.5.2 created 1980 as EC 1.5.99.8, transferred 2013 to EC 1.5.5.2] |
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