Current Microbiology

, Volume 42, Issue 6, pp 442–446 | Cite as

Oxidation of l-Thiazolidine-4-Carboxylate by Δ1-Pyrroline-5-Carboxylate Reductase in Escherichia coli

  • Charles E. Deutch
  • Jessica L. Klarstrom
  • Casey L. Link
  • Dominic L. Ricciardi
Article

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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Copyright information

© Springer-Verlag New York Inc. 2001

Authors and Affiliations

  • Charles E. Deutch
    • 1
  • Jessica L. Klarstrom
    • 2
  • Casey L. Link
    • 1
  • Dominic L. Ricciardi
    • 1
  1. 1.Department of Biological Sciences, University of Nevada, Las Vegas, NV 89154, USAUS
  2. 2.Division of Science and Mathematics, University of Minnesota, Morris, MN 56267, USAUS

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