title: Coenzyme preference of Streptococcus pyogenes δ1-pyrroline-5-carboxylate reductase: evidence supporting NADPH as the physiological electron donor.
abstract: The streptococcal enzyme that catalyzes the last step in proline biosynthesis was heterologously expressed and the recombinant protein was purified to electrophoretic homogeneity and characterized thoroughly. As for δ1-pyrroline-5-carboxylate reductases from other sources, it was able to use either NADH or NADPH as the electron donor in vitro. However, with NADH the activity was markedly inhibited by physiological levels of NADP+. Results also strengthen the possibility that an unusual ordered substrate binding occurs, in which the dinucleotide binds last.
authors.affiliation: Dipartimento di Biologia and Evoluzione, Università di Ferrara, via L. Borsari 46, 44100, Ferrara, Italy.
authors.forename: Davide
authors.initials: D
authors.lastname: Petrollino
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Forlani
mesh_terms: D002384:Catalysis; D007700:Kinetics; D009243:NAD / Q000737:chemistry / Q000378:metabolism*; D009249:NADP / Q000737:chemistry / Q000378:metabolism*; D011392:Proline / Q000096:biosynthesis / Q000378:metabolism; D011762:Pyrroline Carboxylate Reductases / Q000737:chemistry / Q000378:metabolism*; D013297:Streptococcus pyogenes / Q000201:enzymology* / Q000378:metabolism; D013379:Substrate Specificity; D000097502:delta-1-Pyrroline-5-Carboxylate Reductase
chemical_list: D009243:NAD; D009249:NADP; D011392:Proline; D011762:Pyrroline Carboxylate Reductases; D000097502:delta-1-Pyrroline-5-Carboxylate Reductase