PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR THIOL-CONTAINING SERINE PROTEINASE FROM THERMOMYCES-LANUGINOSUS

被引：18

作者：

HASNAIN, S

ADELI, K

STORER, AC

机构：

[1] Institute for Biological Sciences, National Research Council of Canada, Ont., Ottawa

来源：

BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE | 1992年 / 70卷 / 02期

关键词：

THIOL-CONTAINING SERINE PROTEINASE; CHARACTERIZATION; KINETICS; INHIBITOR; SPECIFICITY;

D O I：

10.1139/o92-017

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An extracellular protease produced by the filamentous fungus Thermomyces lanuginosus has been purified and characterized. The results indicate that the enzyme, which we have called humicolin, is a thiol-containing serine protease with a molecular mass of 38000 kilodaltons. Secretion of humicolin, which is glycosylated, is tightly regulated by protein substrates. Kinetic characterization has revealed that humicolin activity is highly dependent upon the deprotonation of a group with a pK(a) of 6.6 and that the enzyme has a specificity for phenylalanine in the P1 position of the substrate.

引用

页码：117 / 122

页数：6