Purification and Characterization of Endo-β-N-acetylglucosaminidase from aFlavobacteriumsp.
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چکیده
منابع مشابه
Transglycosylation 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 کاملPurification and Properties of an Endo-P-iv-acetylglucosaminidase
An enzyme that hydrolyzes di-N-acetylchitobiose linkages in oligosaccharides and glycoproteins was purified to homogeneity from cultural filtrates of Streptomyces griseus. The molecular weight of the enzyme, determined by sedimentation equilibrium analysis, is 27,200 f ZOO, and it appears to consist of a single polypeptide chain. This apparent endo/3-N-acetylglucosaminidase was completely stabl...
متن کاملIntraphagocytic 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 کاملPurification and properties of beta-N-acetylglucosaminidase from Escherichia coli.
beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophenyl-beta-D-2-acetamido-2-deoxyglucopyranoside is 0.43 mM. The molecular weight of this enzyme, determined by bo...
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: Agricultural and Biological Chemistry
سال: 1986
ISSN: 0002-1369
DOI: 10.1080/00021369.1986.10867399