𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Theoretical studies on substrate binding to the active site of carbonic anhydrase

✍ Scribed by Andrzej Sawaryn; W. Andrzej Sokalski

Publisher
John Wiley and Sons
Year
1979
Tongue
English
Weight
299 KB
Volume
16
Category
Article
ISSN
0020-7608

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

The role of some amino acids and metal ions in the catalytic activity of carbonic anhydrase (carbonate dehydratase EC 4.2.1.1) has been investigated. The additional stabilization of the transition state complex was used as the qualitative measure of the effect of molecular surrounding on CO~2~ hydration reaction calculated within the approximate CNDO/2 approach. The effect of the molecular environment has been simulated by inclusion into the SCF LCAO MO Hamiltonian, a term representing the interaction with a set of point charges and atomic dipoles centered on experimentally determined position of Zn^2+^ ion and all atoms of histidine 94, 96, 119 and threonine 199, 200 (or histidine 200 in the case of carbonic anhydrase B). The possible molecular mechanism of CO~2~ hydration inside the active site has been also discussed.

πŸ“œ SIMILAR VOLUMES

Theoretical studies on farnesyl transfer
Theoretical studies on farnesyl transferase: Evidence for thioether product coordination to the active-site zinc sphere
✍ SΓ©rgio Filipe Sousa; Pedro Alexandrino Fernandes; Maria JoΓ£o Ramos πŸ“‚ Article πŸ“… 2007 πŸ› John Wiley and Sons 🌐 English βš– 252 KB

## Abstract Farnesyltransferase (FTase), an interesting zinc metaloenzyme, has been the subject of great attention in anticancer research over the last decade. However, despite the major accomplishments in the field, some very pungent questions on the farnesylation mechanism still persist. In this