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.
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References
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© 1981 Springer-Verlag Berlin Heidelberg
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Snell, E.E., Recsei, P.A. (1981). Bacterial Histidine Decarboxylase and Related Pyruvoyl Enzymes. In: Eggerer, H., Huber, R. (eds) Structural and Functional Aspects of Enzyme Catalysis. Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81738-0_16
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DOI: https://doi.org/10.1007/978-3-642-81738-0_16
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