Abstract
l-Thiazolidine-4-carboxylate (T4C, thiaproline) is a sulfur-containing proline analog that stimulates the immune system in aging mice and inhibits urinary tract pathogens such as Escherichia coli. A constitutive NADP+-dependent T4C dehydrogenase activity was detected in the soluble fraction of a putA::Tn5 mutant of E. coli lacking l-proline dehydrogenase and partially purified by ammonium sulfate precipitation, dye-affinity chromatography on Cibacron Blue 3GA agarose, and ion-exchange chromatography on DEAE-cellulose. At each step in the purification, T4C dehydrogenase activity copurified with Δ1-pyrroline-5-carboxylate (P5C) reductase activity. E. coli strains with greatly reduced P5C reductase activity due to a proC mutation had no detectable T4C dehydrogenase activity. Although P5C reductase did not act on proline, it also catalyzed the oxidation of 3,4-dehydroproline. These results suggest that this biosynthetic enzyme may play a role in the degradation of proline analogs and limit the clinical efficacy of these compounds.
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Received: 14 November 2000 / Accepted: 18 December 2000
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Deutch, C., Klarstrom, J., Link, C. et al. Oxidation of l-Thiazolidine-4-Carboxylate by Δ1-Pyrroline-5-Carboxylate Reductase in Escherichia coli . Curr Microbiol 42, 442–446 (2001). https://doi.org/10.1007/s002840010245
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DOI: https://doi.org/10.1007/s002840010245