| Full text | |
| Author(s): |
Guilherme M. Arantes
[1]
Total Authors: 1
|
| Affiliation: | [1] Universidade de São Paulo. Instituto de Química - Brasil
Total Affiliations: 1
|
| Document type: | Journal article |
| Source: | Química Nova; v. 31, n. 2, p. 377-383, 2008-00-00. |
| Abstract | |
Enzymes are extremely efficient catalysts. Here, part of the mechanisms proposed to explain this catalytic power will be compared to quantitative experimental results and computer simulations. Influence of the enzymatic environment over species along the reaction coordinate will be analysed. Concepts of transition state stabilisation and reactant destabilisation will be confronted. Divided site model and near-attack conformation hypotheses will also be discussed. Molecular interactions such as covalent catalysis, general acid-base catalysis, electrostatics, entropic effects, steric hindrance, quantum and dynamical effects will also be analysed as sources of catalysis. Reaction mechanisms, in particular that catalysed by protein tyrosine phosphatases, illustrate the concepts. (AU) | |