Purification of a 51 kDa endo-β-N-acetylglucosaminidase fromStaphylococcus aureus
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چکیده
منابع مشابه
Purification 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 کاملBacteriolytic enzymes from Staphylococcus aureus. Specificity of ction of endo-beta-N-acetylglucosaminidase.
The bacteriolytic enzyme with an isoelectric point of 9.5 that is produced by all strains of Staphylococcus aureus investigated was purified from strain M18 (Wadström & Hisatsune, 1970). This enzyme released reducing groups from cell walls of Micrococcus lysodeikticus and was thus shown to be a bacteriolytic hexosaminidase. Although dinitrophenylation and acid hydrolysis of cell walls hydrolyse...
متن کاملPurification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.
The DNA region encoding the mature form of a pneumococcal murein hydrolase (LytB) was cloned and expressed in Escherichia coli. LytB was purified by affinity chromatography, and its activity was suggested to be the first identified endo-beta-N-acetylglucosaminidase of Streptococcus pneumoniae. LytB can remove a maximum of only 25% of the radioactivity from [(3)H]choline-labeled pneumococcal cel...
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: FEMS Microbiology Letters
سال: 1989
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1989.tb03635.x