Contribution to Catalysis and to Stability of the Essential Cysteine Residue at the Active Site ofd-Glucosaminate Dehydratase fromPseudomonas fluorescens
Abstract:Chemical modification of purified o-glucosaminate dehydratase (GADH) apoenzyme by N-ethylmaleimide (NEM) and by 7-chloro-4-aminobenzo-2-oxa-l,3-diazole (NBDCI) resulted in the time-and concentration-dependent inactivation of the enzyme in each case. The inactivation followed pseudo-first-order kinetics and a double-logarithmic plot of the observed pseudo-first-order rate constant against reagent concentration proved evidence for an approximately first-order reaction, suggesting that the modification of a singl… Show more
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