Abstract
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) |
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Pages (from-to) | 2825-2828 |
Number of pages | 4 |
Journal | Biochemistry |
Volume | 18 |
Issue number | 13 |
DOIs | |
State | Published - 1979 |
All Science Journal Classification (ASJC) codes
- Biochemistry