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) |
|---|---|
| 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
Fingerprint
Dive into the research topics of 'Stereochemical Course of the Reaction Catalyzed by 5‘-Nucleotide Phosphodiesterase from Snake Venom'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver