N-glycan breakdown by bacterial CAZymes

被引:8
作者
Crouch, Lucy I. [1 ]
机构
[1] Univ Birmingham, Inst Microbiol & Infect, Coll Med & Dent Sci, Birmingham B15 2TT, England
基金
英国惠康基金;
关键词
STREPTOCOCCUS-PNEUMONIAE; SIALIC-ACID; ACETYLGLUCOSAMINIDASE; ENDOGLYCOSIDASE; OLIGOSACCHARIDES; IDENTIFICATION; RECOGNITION; SPECIFICITY; METABOLISM; HYDROLYZE;
D O I
10.1042/EBC20220256
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
The modification of proteins by N-glycans is ubiquitous to most organisms and they have multiple biological functions, including protecting the adjoining protein from degradation and facilitating communication or adhesion between cells, for example. Microbes have evolved CAZymes to deconstruct different types of N-glycans and some of these have been characterised from microbes originating from different niches, both commensals and pathogens. The specificity of these CAZymes provides clues as to how different microbes breakdown these substrates and possibly cross-feed them. Discovery of CAZymes highly specific for N-glycans also provides new tools and options for modifying glycoproteins.
引用
收藏
页码:373 / 385
页数:13
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