Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of the present study was to establish the effect of the carcinogen 1,2 dimethylhydrazine on the activities of the jejunal glucosidases and to assess the possible modifying effect of different diets. Two control groups of Wistar albino rats were used - fed standard pellet diet and fed the same diet + 1,2 dimethylhydrazine treatment. Six experimental groups treated with 1,2 dimethylhydrazine were provided. One of them was fed standard diet, containing 30% of wheaten bran and the other 5 groups received high-lipid diets, containing 30% of different fats. The rats were injected subcutaneously once a week for 12 weeks with 20 mg 1,2 dimethylhydrazine/kg b.m. and left for 12 weeks in order to develop a tumor growth. The activities of 5 glucosidases (lactase, maltase, sucrase, palatinase and cellobiase) were determined in homogenates from jejunal mucosa taken near by the tumors and in homogenates from the tumors themselves. An expressed decrease of the jejunal glucosidase activities near the tumors and in the tumors was established. The animals fed 30% wheaten bran diet did not develop tumorigenesis and showed comparatively slight decrease of the enzyme activities. In general, the high-fat regimens did not exert such a preventive effect.
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PMID:Changes in the activities of jejunal glucosidases in experimental intestinal tumorigenesis induced by 1,2 dimethylhydrazine in rats fed different diets. 191 61

Beta-glucosidases constitute a major group among glycosylhydrolase enzymes. Out of the 82 families classified under glycosylhydrolase category, these belong to family 1 and family 3 and catalyze the selective cleavage of glucosidic bonds. This function is pivotal in many crucial biological pathways, such as degradation of structural and storage polysaccharides, cellular signaling, oncogenesis, host-pathogen interactions, as well as in a number of biotechnological applications. In recent years, interest in these enzymes has gained momentum owing to their biosynthetic abilities. The enzymes exhibit utility in syntheses of diverse oligosaccharides, glycoconjugates, alkyl- and aminoglucosides. Attempts are being made to understand the structure-function relationship of these versatile biocatalysts. Earlier reviews described the sources and properties of microbial beta-glucosidases, yeast beta-glucosidases, thermostable fungal beta-glucosidase, and the physiological functions, characteristics, and catalytic action of native beta-glucosidases from various plant, animal, and microbial sources. Recent efforts have been directed towards molecular cloning, sequencing, mutagenesis, and crystallography of the enzymes. The aim of the present article is to describe the sources and properties of recombinant beta-glucosidases, their classification schemes based on similarity at the structural and molecular levels, elucidation of structure-function relationships, directed evolution of existing enzymes toward enhanced thermostability, substrate range, biosynthetic properties, and applications.
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PMID:Microbial beta-glucosidases: cloning, properties, and applications. 1248 26