Altering the specificity of subtilisin B. lentus by combining site-directed mutagenesis and chemical modification

• The thiol side chain of the M222C mutant of the subtilisin from Bacillus lentus (SBL) has been chemically modified by methyl-, aminoethyl-, and sulfonatoethylthiosulfonate reagents. Introduction of charged residues into the active site of the enzyme reduced the catalytic efficiency with Suc-AAPF-pNA as the substrate, but resulted in better binding of sterically demanding boronic acid inhibitors.

Subject headings

TEKNIK OCH TEKNOLOGIER  -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)

ENGINEERING AND TECHNOLOGY  -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)

Keyword

boronic acid derivative

subtilisin

article

Eggerthella lenta

enzyme activity

enzyme modification

site directed mutagenesis

Bacillus lentus

Publication and Content Type

ref (subject category)

art (subject category)