CP40 from Corynebacterium pseudotuberculosis is an endo-β-N-acetylglucosaminidase
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چکیده
منابع مشابه
Intraphagocytic Β-n-acetylglucosaminidase
The beta-N-acetylglucosaminidases of rabbit and human polymorphonuclear leukocytes and of rabbit alveolar macrophages have been studied in comparison with the beta-N-acetylglucosaminidase derived from a soil bacillus which had previously been shown to hydrolyze the group-specific polysaccharide of Group A streptococci. The phagocytic enzymes are lysosome associated and have an acid pH optimum. ...
متن کاملTransglycosylation Activity of Glycosynthase Mutants of Endo-β-N-Acetylglucosaminidase from Coprinopsis cinerea
Endo-β-N-acetylglucosaminidase (ENGase), which catalyzes hydrolysis of N-linked oligosaccharides, is a useful tool for analyzing oligosaccharide contents of glycoproteins. However, there are only a few known ENGases that can catalyze the hydrolysis of human complex type oligosaccharides, and although commercially available, they are expensive. Here, we report the cloning of two ENGase encoding ...
متن کاملCorynebacterium pseudotuberculosis cp09 mutant and cp40 recombinant protein partially protect mice against caseous lymphadenitis
BACKGROUND Caseous lymphadenitis (CLA) is an infectious disease that affects small ruminants and is caused by Corynebacterium pseudotuberculosis. This disease is responsible for high economic losses due to condemnation and trim of infected carcasses, decreased leather and wool yield, loss of sales of breeding stock and deaths from internal involvement. Treatment is costly and ineffective; the m...
متن کاملStructural Basis and Catalytic Mechanism for the Dual Functional Endo-β-N-Acetylglucosaminidase A
Endo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become the focus of intense research because of their potential for synthesis of glycopeptides. We have determined the 3D structures of an ENGase from Arthrobacter protophormiae (Endo-A) in 3 forms, one in native form, on...
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ژورنال
عنوان ژورنال: BMC Microbiology
سال: 2016
ISSN: 1471-2180
DOI: 10.1186/s12866-016-0884-3