Abstract
Simple zinc complexes of glycine, histidine, and cysteine are proposed as evolutionary models for hydrolytic enzymes. Catalytic activity of (amino acidato)zinc complexes has been studied towards hydrolysis of 4-nitrophenyl phosphate at 40 °C over the pH range 5.0—10.0 by monitoring release of p-nitrophenol at 405 nm. Detailed kinetic investigations on hydrolysis of ester catalyzed by zinc complexes are discussed through formation of (amino acidato)zinc-substrate complex. Mechanistic and evolutionary aspect of this study are discussed in relation to the esterase property of the zinc metalloenzymes.
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