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.
KeywordsSulfhydryl Group Pyruvic Acid Native Enzyme Subunit Structure Histidine Decarboxylase
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