Searching for the Lowest Energy Conformation of Substrates in the Carboxypeptidase A Active Site Using Monte Carlo/Energy Minimization Techniques
✍ Scribed by Guiqing Liang; John F. Sebastian
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 326 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0045-2068
No coin nor oath required. For personal study only.
✦ Synopsis
More than fifteen substrates of carboxypeptidase A (CPA) have been ''docked'' to the active site of the enzyme and searched for the lowest energy conformation of the substrates bound to the active site. The method employed combines Monte Carlo procedures with energy minimization (MC/EM procedures). The distances of P 1Ј -P 3 to S 1Ј -S 3 were measured. The computational results are consistent with the proposed binding interactions of CPA and its substrates and also with the promoted-water pathway of CPA catalysis. This study has demonstrated that MC/EM procedures are very useful for searching the conformations of substrates available in the active site of the enzyme.