| pubmed-article:9439628 | pubmed:abstractText | Although angiotensin (ANG)-I is a substrate sensitive to chymase, the cleavage site differs among the chymase families. While human chymase (HC) hydrolyses the Phe8-His9 bond of ANG-I to ANG-II, rat chymase (RMCP-I) degrades the Tyr4-Ile5 bond of ANG-I to the inactive fragments. To clarify this different catalysis for ANG-I at the atomic level, three-dimensional structures of HC and RMCP-I were constructed by the molecular dynamic simulation. The energy-refined models clearly showed the significant difference in the electrostatic potential of the solvent surface. From the modeling study of their complex structures with ANG-I, the functional difference between both enzymes was clearly related with the electrostatic difference, especially at the C-terminal substrate-binding site. | lld:pubmed |
