The Substrate Versatility of Δ¹-Pyrroline-5-carboxylate Reductase (ProC) from <i>Escherichia coli</i>.

ABSTRACT: 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 Escherichia coli 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 an

SUBMITTER: Polverini E 

PROVIDER: S-EPMC12899673 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature