Almost one-third of all proteases can be classified as serine proteases, named for the
nucleophilic Ser residue at the active site. This mechanistic class was originally …

Proteases or proteolytic enzymes form one of the largest and more important groups of
enzymes. Proteases selectively catalyze the hydrolysis of peptide bonds and can be divided …

Abstract Structure‐based mutational analysis of serine protease specificity has produced a
large database of information useful in addressing biological function and in establishing a …

A computer program is used to analyse automatically and objectively the atomic co-
ordinates of a large number of globular proteins in order to identify the regions of α-helix, β …

Oligonucleotide-directed mutagenesis was used to investigate the nature of transition state
stabilization in the catalytic mechanism of the serine protease, subtilisin BPN'. The gene for …

A survey of known protein structures reveals that approximately 70% of serine residues and
at least 85%(potentially 100%) of threonine residues in helices make hydrogen bonds to …

Site-directed mutagenesis is a very powerful approach to altering the biological functions of
proteins, the structural stability of proteins and the interactions of proteins with other …

Fig. 2. Diagram showing the rate-limiting acylation step (which defines kcat) for hydrolysis of
peptide bonds by subtilisin BPN'. For subtilisin BPN', deacylation is> 33 times faster than …

Structural studies on serine proteinases have shown that hydrogen bonds are involved in
stabilizing the charged tetrahedral intermediate in the transition-state complex. However …

Steric and hydrophobic effects on substrate specificity were probed by protein engineering
of subtilisin. Subtilisin has broad peptidase specificity and contains a large hydrophobic …