标题:Extracellular metalloproteases from bacteria
作者:Wu, Ji-Wei; Chen, Xiu-Lan
作者机构:[Wu, Ji-Wei; Chen, Xiu-Lan] Shandong Univ, State Key Lab Microbial Technol, Marine Biotechnol Res Ctr, Jinan 250100, Peoples R China.; [Wu, Ji-Wei] 更多
通讯作者:Chen, XL
通讯作者地址:[Chen, XL]Shandong Univ, State Key Lab Microbial Technol, Marine Biotechnol Res Ctr, Jinan 250100, Peoples R China.
来源:APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
出版年:2011
卷:92
期:2
页码:253-262
DOI:10.1007/s00253-011-3532-8
关键词:Bacterial extracellular metalloproteases; Diversity; Structural; characteristics; Maturation mechanisms; Properties; Applications
摘要:Bacterial extracellular metalloproteases (BEMPs) are a large group of metal-containing proteases secreted by heterotrophic bacteria. In this review, the diversity, structural characteristics, mechanisms of maturation, physiological roles, and applications of BEMPs are described. BEMPs are distributed among nine families of metalloproteases because of differences in primary sequences and structural characteristics. Until now, all of the BEMPs identified have been endoproteases harboring one catalytic Zn2+ in the active centers. BEMPs are usually synthesized as inactive zymogens with a propeptide that is covalently linked to and inhibits the catalytic domain. The removal of the propeptides of BEMPs is dependent on other proteases or an autocleavage process. The main physiological function of BEMPs is to degrade environmental proteins and peptides for bacterial heterotrophic nutrition. As extracellular proteases, BEMPs vary greatly in enzymology properties to adapt to their respective environments. BEMPs have been widely used in the food and pharmaceutical industries. In order to broaden the application of BEMPs, it is essential to explore novel BEMPs and apply gene/protein engineering to improve the production and properties of promising BEMPs.
收录类别:EI;SCOPUS;SCIE
WOS核心被引频次:32
Scopus被引频次:35
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-82455199191&doi=10.1007%2fs00253-011-3532-8&partnerID=40&md5=0e5774acda49f0f26b3e97018e3e1020
TOP