Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Microbial endoglycosidases are useful for elucidating the structure and function of the oligosaccharide chains of glycoconjugates. Most of the microbial endo-beta-N-acetylglucosaminidases including Endo-H can preferentially act on high-mannose type chains of asparagine-linked oligosaccharides of various glycoproteins. Among them, Flavobacterium sp. enzyme is produced in large amounts by the inducing cultivation. Using this enzyme, the role of oligosaccharide chains in various microbial glycoenzymes such as Rhizopus glucoamylase, and yeast invertase was examined. The findings suggested that the oligosaccharide chains of them are essential participants in the stabilization of the enzyme and in the protection from proteolytic inactivation. Novel endo-beta-N-acetylglucosaminidases were also found in the culture broths of microorganisms. Unlike most microbial endo-beta-N-acetylglucosaminidases, Endo-M of Mucor hiemalis could act on a complex type oligosaccharide chains, which is similar to Endo-F2 in multiple form of Endo-F from Flavobacterium meningosepticum. The complete amino acid sequences of Endo-F1, -F2, -F3, -H, and Flavobacterium sp. enzyme were determined. All of them had two highly conserved regions common to a number of chitinases. Endo-alpha-N-acetylgalactosaminidase which hydrolyzes the O-glycosidic linkages in glycoproteins was found in the culture broth of only a few microorganisms. The production of Alcaligenes sp. enzyme was highly induced by the addition of porcine gastric mucin in the culture medium. There is some evidence that endo-alpha-N-acetylgalactosaminidases may recognize not only the glycon but also the aglycon amino acids.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Microbial endoglycosidases for analyses of oligosaccharide chains in glycoproteins. 782 34

A scheme has been developed for isolation and purification of the enzyme with alpha-N-acetylgalactosaminidase and alpha-galactosidase activities which included fractionation by ammonium sulphate and chromatography on TSK-gels Toyopearl HW-60 and Fractogel DEAE-650-s and Sepharose 6B. The enzyme was purified 600 times with the yield of 28%. The enzyme preparation did not contain fucosidase, invertase and proteolytic activities. Molecular mass of the enzyme from the data of gel-filtration on Sepharose 6B was 430 kDa, according to the data of electrophoresis in DS-PAAG--70 kDa. It is shown that acidic and hydrophobic aminoacids prevail in the enzyme molecule, the carbohydrate component containing galactose, mannose, glucosamine and two nonidentified hexosamines is also present there. The enzyme preparation is stable during 48 hours at 20 degrees C; its pH-optimum is at pH 3.5-4.1. Michaelis constants concerning n-nitrophenyl-alpha-N-acetylgalactopyranoside and n-nitrophenyl-alpha-D-galactopyranoside were 1.18 and 1.25 mM, respectively.
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PMID:[Purification and physico-chemical properties of glycosidase of Aspergillus niger 185sh]. 1507 44