Revised Manuscript Received February 4, 1994® abstract: The S'subsite specificity of four
homologous serine proteases, rat chymotrypsin, rat trypsin,-lytic protease, and cercarial …

α-Lytic protease is a homologue of the mammalian serine proteases such as trypsin,
chymotrypsin, and elastase, and its single histidine residue belongs to the Asp-His-Ser …

The hydrolytic cleavage of peptide bonds by proteases is an ancient biochemical reaction
prevalent in all forms of living organisms. Hydrolysis of a peptide substrate by a protease …

Revised Manuscript Received July 27, 1989 abstract: Active site serine 195 of rat anionic
trypsin was replaced with a cysteine by site-specific mutagenesis in order to determine if a …

A messenger RNA encoding a chymotrypsin-like preproprotease is expressed abundantly
and specifically in the distal quarter of the intestine of the molluse Haliotis rufescens (red …

One of the enduring paradigms in enzymology is the theme of evolutionary divergence in
substrate specificity from a parental enzyme possessing a prototypical fold. Within the fold of …

The naturally occurring serine protease inhibitor, chymostatin, forms a hemiacetal adduct
with the catalytic Ser195 residue of Streptomyces griseus protease A. Restrained parameter …

Although the subject of many studies, detailed structural information on aspects of the
catalytic cycle of serine proteases is lacking. Crystallographic analyses were performed in …

MATERIALS AND METHODS Enzymes. Bovine-chymotrypsin (lyophilized, analytical grade,
lot 10860521-39, Boehringer, Mannheim, Germany) and bovinetrypsin (lyophilized …

Trypsin mutant Asp189Ser, first described by Gráf et al.[Gráf, L., Jancsó, Á., Szilágyi, L.,
Hegyi, G., Pintér, K., Náray‐Szabó, G., Hepp, J., Medzihradszky, K. & Rutter, WJ (1988) Proc …