{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["31(3)"],"submitter":["Polverini E"],"pubmed_abstract":["Δ<sup>1</sup>-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 an"],"journal":["Molecules (Basel, Switzerland)"],"pagination":["501"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12899673"],"repository":["biostudies-literature"],"pubmed_title":["The 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;."],"pmcid":["PMC12899673"],"pubmed_authors":["Pastori A","Polverini E","Vecchi A","Capra G","Peracchi A"],"additional_accession":[]},"is_claimable":false,"name":"The 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;.","description":"Δ<sup>1</sup>-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 an","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-06T03:22:29.89Z","creation":"2026-07-06T03:11:12.988Z"},"accession":"S-EPMC12899673","cross_references":{"pubmed":["41683478"],"doi":["10.3390/molecules31030501"]}}