Bacterial Histidine Decarboxylase and Related Pyruvoyl Enzymes

  • E. E. Snell
  • P. A. Recsei
Part of the Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden book series (MOSBACH, volume 32)

Abstract

Enzymes that contain a covalently bound, catalytically essential pyruvoyl residue were first reported between 1967 and 69 by Hodgins and Abeles [1], and by Riley and Snell [2], Hodgins and Abeles used partially purified preparations of D-proline reductase from Clostridium stick-landii. This enzyme catalyzes the conversion of D-proline to δ-amino valerate; some of its properties are shown in Table 1. The essential carbonyl group in this enzyme was identified by reduction with tritium- labeled NaBH4, followed by isolation and characterization of tritiated lactic acid from acid hydrolysates of the enzyme preparation. A mechanism that involves formation of a protonated Schiff’s base or carbinolamine between the pyruvoyl residue of the enzyme and its substrate was postulated, but no evidence for this postulate has appeared.

Keywords

Hydrolysis Titration Pyridine Adduct Serine 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1981

Authors and Affiliations

  • E. E. Snell
  • P. A. Recsei
    • 1
    • 2
  1. 1.Department of MicrobiologyThe University of Texas at AustinAustinUSA
  2. 2.Department ChemistryThe University of Texas at AustinAustinUSA

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