Stereochemical Course of the Reaction Catalyzed by 5‘-Nucleotide Phosphodiesterase from Snake Venom

Floyd R. Bryant, Stephen Benkovic

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The hydrolysis reaction of ATPαS by snake venom phosphodiesterase is highly specific for the B diastereomer and proceeds with 88% retention of configuration at phosphorus. Since this enzyme also catalyzes the hydrolysis of the S enantiomer of O-p-nitrophenyl phenylphosphonothioate, the absolute configuration at Pα of ATPαS (B) is assigned as the R configuration provided the two substrates are processed identically. A mechanism for the hydrolysis reactions catalyzed by the venom phosphodiesterase involving at least a single covalent phosphoryl-enzyme intermediate is in accord with this result.

Original languageEnglish (US)
Pages (from-to)2825-2828
Number of pages4
Issue number13
Publication statusPublished - Jan 1 1979


All Science Journal Classification (ASJC) codes

  • Biochemistry

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