The Enzyme Database

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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, 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. [PMID: 22040654]
[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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