The nature of enzyme catalysis in trypsin.

AUTOR(ES)

Weiner, S J

RESUMO

We present a combined quantum/molecular mechanical study of the trypsin-catalyzed hydrolysis of a specific tripeptide substrate, including the entire enzyme in the calculation, as well as 200 H2O molecules. The results illustrate how the enzyme and nearby H2O molecules stabilize the ionic intermediates in peptide hydrolysis, such that the reaction is calculated to have a barrier that is significantly smaller than the calculated and experimental base-catalyzed barrier of formamide hydrolysis in aqueous solution. This enables us to understand how serine proteases increase the rates for reactions that take place in their active sites, compared to the corresponding rates for analogous solution reactions.

Documentos Relacionados

• Feedback regulation of pancreatic enzyme secretion. Suppression of cholecystokinin release by trypsin.
• Rotavirus isolation and cultivation in the presence of trypsin.
• Electrostatic complementarity within the substrate-binding pocket of trypsin.
• Simian rotavirus SA-11 plaque formation in the presence of trypsin.
• Immunofluorescence staining of adenovirus in fixed tissues pretreated with trypsin.