Abstract
Arginase from Phaseolus vulgaris was inactivated by diethyl pyrocarbonate (DEPC). The bimolecular rate constant for inactivation by DEPC was 1300 M −1 min −1 and the reaction order with respect to DEPC concentration was ca 1. The inactivation followed a titration curve for a residue with a p K a of 6.7±0.1 at 25° and the enzymatic activity was completely restored by hydroxylamine. Results are taken as evidence for a critical, but not essential, histidine residue in the enzyme.
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