Bacterial Histidine Decarboxylase and Related Pyruvoyl Enzymes
Enzymes that contain a covalently bound, catalytically essential pyruvoyl residue were first reported between 1967 and 69 by Hodgins and Abeles , and by Riley and Snell , 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.
KeywordsHydrolysis Titration Pyridine Adduct Serine
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