Enzymatic properties of the purified putA protein from Salmonella typhimurium.
In the previous paper (Menzel, R., and Roth, J. (1981) J. Biol. Chem. 256, 9755-9761) we have described the purification of a protein, the putA gene product, which has both proline oxidase and pyrroline-5-carboxylic acid dehydrogenase activities. In this paper we demonstrate that these enzyme activities are distinct with respect to a number of characteristics. The oxidase activity proceeds by a ping-pong mechanism involving the reduction of an enzyme-bound flavin. The dehydrogenase activity utilizes an ordered reaction mechanism.
D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D001426:Bacterial Proteins / Q000378:metabolism*; D007700:Kinetics; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D011394:Proline Oxidase / Q000378:metabolism*; D011762:Pyrroline Carboxylate Reductases / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000201:enzymology*; D013053:Spectrophotometry; D013379:Substrate Specificity
D001426:Bacterial Proteins; D050842:1-Pyrroline-5-Carboxylate Dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011762:Pyrroline Carboxylate Reductases; D011394:Proline Oxidase