A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor . In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 184.108.40.206, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria.
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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]
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 220.127.116.11 created 1980 as EC 18.104.22.168, transferred 2013 to EC 22.214.171.124]