Revised Manuscript Received July 19, 1993® abstract: The mature form of subtilisin is an
unusual example of a monomeric protein with a high kinetic barrier to folding and unfolding …

The functional role of the negatively charged amino acid residue in subtilisin J from Bacillus
stearothermophilus has been investigated by site-directed mutagenesis. Glu-195 located at …

The N-terminal pro-peptide of 77 amino acid residues is essential for the folding of subtilisin,
an alkaline serine protease from Bacillus subtilis. The synthetic pro-peptide has been shown …

Objectives A bacterial halotolerant enzyme was characterized to understand the molecular
mechanism of salt adaptation and to explore its protein engineering potential. Results …

Ak. 1 protease, a thermostable subtilisin isolated originally from Bacillus st. Ak. 1, was
purified to homogeneity from the Escherichia coli clone PB5517. It is active against …

Subtilisin E was rationally engineered to improve its stability in polar organic solvents such
as dimethylformamide (DMF). A charged surface residue, Asp248, was substituted by three …

Differences in salt bridges are believed to be a structural hallmark of homologous enzymes
from differently temperature-adapted organisms. Nevertheless, the role of salt bridges on …

Variants designed using PROTEUS have been produced in an attempt to engineer
stabilizing salt bridges into subtilisin BPN'. All the mutants constructed by site-directed …

Thermodynamic stability of an alkaline protease from a new alkaliphilic Nesterenkonia sp.
AL-20, was investigated and compared with that of Subtilisin Carlsberg. The amount of …

Subtilisin from a wide variety of Bacillus species has been extensively investigated as a
promising target for protein engineering. In this study, we analyzed the substrate specificity …