The Thermolysin Family (M4) of Enzymes: Therapeutic and Biotechnological Potential

被引：139

作者：

Adekoya, Olayiwola A. ^{[1
]}

Sylte, Ingebrigt ^{[1
]}

机构：

[1] Univ Tromso, Fac Med, Inst Med Biol, Dept Pharmacol, N-9037 Tromso, Norway

来源：

CHEMICAL BIOLOGY & DRUG DESIGN | 2009年 / 73卷 / 01期

关键词：

cold adaptation; drug design; drug discovery; molecular modeling; thermolysin; PSEUDOMONAS-AERUGINOSA ELASTASE; STREPTOMYCES METALLOPROTEINASE INHIBITOR; CATALYZED PEPTIDE-SYNTHESIS; TRANSITION-STATE ANALOGS; PROTEASE-ENCODING GENE; NEUTRAL PROTEASE; ACTIVE-SITE; SUBSTRATE-SPECIFICITY; STRUCTURAL-ANALYSIS; CRYSTAL-STRUCTURE;

D O I：

10.1111/j.1747-0285.2008.00757.x

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：

Zinc containing peptidases are widely distributed in nature and have important roles in many physiological processes. M4 family comprises numerous zinc-dependent metallopeptidases that hydrolyze peptide bonds. A large number of these enzymes are implicated as virulence factors of the microorganisms that produce them and are therefore potential drug targets. Some enzymes of the family are able to function at the extremes of temperatures, and some function in organic solvents. Thereby enzymes of the thermolysin family have an innovative potential for biotechnological applications.

引用

页码：7 / 16

页数：10

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