biostudies-literatureUnknown31(3)Polverini EΔ¹-Pyrroline-5-carboxylate reductase (EC 1.5.1.2; called ProC in most bacteria) is an enzyme of central metabolism that catalyzes the last step of the proline biosynthetic pathways, namely the NADPH-dependent reduction of pyrroline-5-carboxylate (P5C) to L-proline (L-Pro). The enzyme, however, is also active towards other substrates, and these reactions might have physiological relevance. Herein, the substrate versatility of ProC from <i>Escherichia coli</i> was explored as follows. We initially characterized the reverse reaction carried out by ProC, i.e., the formation of P5C from L-Pro. This reaction was easily measurable at pH 10, allowing the determination of the kinetic parameters. Under the same conditions, we then tested the ability of ProC to oxidize a number of L-Pro anMolecules (Basel, Switzerland)501https://www.ebi.ac.uk/biostudies/studies/S-EPMC12899673biostudies-literatureThe Substrate Versatility of Δ&lt;sup&gt;1&lt;/sup&gt;-Pyrroline-5-carboxylate Reductase (ProC) from &lt;i&gt;Escherichia coli&lt;/i&gt;.PMC12899673Pastori APolverini EVecchi ACapra GPeracchi AfalseThe Substrate Versatility of Δ&lt;sup&gt;1&lt;/sup&gt;-Pyrroline-5-carboxylate Reductase (ProC) from &lt;i&gt;Escherichia coli&lt;/i&gt;.Δ¹-Pyrroline-5-carboxylate reductase (EC 1.5.1.2; called ProC in most bacteria) is an enzyme of central metabolism that catalyzes the last step of the proline biosynthetic pathways, namely the NADPH-dependent reduction of pyrroline-5-carboxylate (P5C) to L-proline (L-Pro). The enzyme, however, is also active towards other substrates, and these reactions might have physiological relevance. Herein, the substrate versatility of ProC from <i>Escherichia coli</i> was explored as follows. We initially characterized the reverse reaction carried out by ProC, i.e., the formation of P5C from L-Pro. This reaction was easily measurable at pH 10, allowing the determination of the kinetic parameters. Under the same conditions, we then tested the ability of ProC to oxidize a number of L-Pro an2026-01-01T00:00:00Z2026 Jan2026-07-06T03:22:29.89Z2026-07-06T03:11:12.988ZS-EPMC128996734168347810.3390/molecules31030501