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

被引：18

作者：

Berglund, P

Stabile, MR

Gold, M

Jones, JB

Mitchinson, C

Bott, RR

Graycar, TP

机构：

[1] UNIV TORONTO,DEPT CHEM,TORONTO,ON M5S 3H6,CANADA

[2] UNIV TORONTO,DEPT MOL & MED GENET,TORONTO,ON M5S 3H6,CANADA

[3] GENENCOR INT INC,PALO ALTO,CA 94304

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1996年 / 6卷 / 21期

关键词：

D O I：

10.1016/0960-894X(96)00467-2

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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. Copyright (C) 1996 Elsevier Science Ltd

引用

页码：2507 / 2512

页数：6

共 26 条

[1] CHEMICAL MODIFICATIONS OF A CYSTEINYL RESIDUE INTRODUCED IN THE BINDING-SITE OF CARBOXYPEPTIDASE-Y BY SITE-DIRECTED MUTAGENESIS [J].