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 language||English (US)|
|Number of pages||4|
|State||Published - 1979|
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