STEREOCHEMICAL COURSE OF THE REACTION CATALYZED BY 5'-NUCLEOTIDE PHOSPHODIESTERASE FROM SNAKE-VENOM

被引：150

作者：

BRYANT, FR ^{[1
]}

BENKOVIC, SJ ^{[1
]}

机构：

[1] PENN STATE UNIV,DEPT CHEM,UNIVERSITY PK,PA 16802

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 13期

关键词：

D O I：

10.1021/bi00580a022

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. © 1979, American Chemical Society. All rights reserved.

引用

页码：2825 / 2828

页数：4