Abstract
Snake venom phosphodiesterase fromCrotalus adamanteus can be purified by blue sepharose chromatography followed by gel exclusion chromatography on Sephadex G-100. The enzyme is judged to be homogeneous by SDS gel electrophoresis. Atomic absorption spectrometry indicates a stoichiometry of 1.07 g-atom of zinc per mole of purified enzyme. The enzyme is inhibited by a wide variety of structurally different metal binding agents, e.g., 1,10-phenanthroline, thioglycolic acid,l-cysteine, 8-hydroxy-5-quinoline sulfonic acid, EDTA, and dipicolinic acid. The results of both the chelator inhibition and the atomic absorption analysis indicate that snake venom phosphodiesterase is a zinc metalloenzyme. Snake venom phosphodiesterase shares a number of mechanistic features in common with the nucleotidyl transferases. All of these enzymes contain zinc, are activated by magnesium, and catalyze α-β phosphoryl bond cleavage. Mechanistic studies of phosphodiesterase may therefore be helpful in understanding the mechanism of the hydrolytic step catalyzed by all of these enzymes.
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