Stereochemical course of the reaction catalyzed by 5'-nucleotide phosphodiesterase from snake venom.
The hydrolysis reaction of ATP alpha S 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 enantimoer of O-p-nitrophenyl phenylphosphonothioate, the absolute configuration at A alpha of ATP alpha S (B) is assigned as the R configuration provided the two substrates are processed identically. A mechanism for the hydrolysis reactions catalzyed by the venom phosphodiesterase involving at least a single covalent phosphoryl-enzyme intermediate is in accord with this result.
D003435:Crotalid Venoms / Q000378:metabolism*; D007553:Isotope Labeling / Q000379:methods; D009708:Nucleotidases / Q000378:metabolism*; D010103:Oxygen Isotopes; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D013379:Substrate Specificity
D003435:Crotalid Venoms; D010103:Oxygen Isotopes; D009708:Nucleotidases; D010727:Phosphoric Diester Hydrolases