EXTENDING CRYSTALLOGRAPHIC INFORMATION WITH SEMIEMPIRICAL QUANTUM-MECHANICS AND MOLECULAR MECHANICS - A CASE OF ASPARTIC PROTEINASES

被引：5

作者：

GOLDBLUM, A

RAYAN, A

FLIESS, A

GLICK, M

机构：

[1] Department of Pharmaceutical Chemistry, School of Pharmacy, Hebrew University of Jerusalem, Jerusalem

来源：

JOURNAL OF CHEMICAL INFORMATION AND COMPUTER SCIENCES | 1993年 / 33卷 / 02期

关键词：

D O I：

10.1021/ci00012a014

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The results of crystallographic analysis of a complex between an aspartic proteinase, endothiapepsin, and an inhibitor have been extended through the assignment of protons in the active site, to study various steps in the reaction with a substrate. Mechanistic implications are suggested as a consequence of semiempirical quantum mechanical calculations, indicating that most of the activation energy is required to bring the substrate from an initial binding mode to close distance to a water molecule.

引用

页码：270 / 274

页数：5

共 12 条

[1]

Dunn B.M., 1991, ADV EXPT MED BIOL, V306

[2] IMPROVEMENT OF THE HYDROGEN-BONDING CORRECTION TO MNDO FOR CALCULATIONS OF BIOCHEMICAL INTEREST [J].