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)

Polymorphonuclear leucocytes were isolated from pig blood relatively free from other cells and were characterised biochemically and morphologically and compared with human PMNLs. The activities of 16 enzymes of porcine and human PMNLs were measured and compared. Alkaline phosphatase, acid phosphatase, phosphodiesterase, gamma-glutamyl transpeptidase, NADH-cytochrome c oxidoreductase, malate dehydrogenase and acetylcholinesterase had higher specific activities in procine than in human cells. Alkaline phosphatase has an 87-fold higher specific activity in porcine than in human cells. beta-glucuronidase, lysozyme, beta-galactosidase, N-acetyl-glucosaminidase, beta-glucosidase, myeloperoxidase and catalase had higher specific activities in human than in porcine cells. beta-glucuronidase and myeloperoxidase showed over a 1000- and a 13-fold higher specific activity, respectively, in human than in porcine cells. Porcine PMNLs are readily available in large numbers and are recommended for studies of phagocytosis, chemotaxis and membrane biochemistry.
 ...
PMID:Biochemical characterisation of porcine polymorphonuclear leucocytes: comparison with human polymorphonuclear leucocytes. 687 22

Peroxidases (E.C. 1.11.1.7., hydrogen donor oxidoreductase) utilize hydrogen peroxide or substituted peroxides for the oxidation of a large number of substrates. Peroxidases are widely distributed and have been isolated from many higher plants (1). The wide distribution of the enzyme suggests that it could be of great biological importance, but the physiological functions and metabolic control of these enzymes are still poorly understood. The simultaneous presence of amine oxidase and peroxidase in cell walls suggests that the peroxide generated on oxidation of the amines could be utilized by the peroxidase (2,3). Recently we have purified an amine oxidase from Hordeum vulgare (4) and we have attempted to purify the peroxidase in order to study in vitro the reconstituted coupled system. beta-glucosidase (beta-D-glucoside glucohydrolase E.C. 3.2.1.21.) is capable of transforming glucosides in glucose and the corresponding aglycone or disaccharides as cellobiose, sophorose, gentiobiose. This enzyme is widely distributed in plants, fungi, bacteria, yeasts and animals (5,6). In the homogenate of Hordeum vulgare seedlings we also found beta-glucosidase activity and also attempted to purify beta-glucosidase. This enzyme copurified with peroxidase up to the last step. We report here the isolation of peroxidase and beta-glucosidase from Hordeum vulgare seedlings: some molecular and kinetic properties are given.
 ...
PMID:Improved chromatographic purification of peroxidase and beta-glucosidase from Hordeum vulgare seedlings. 824 30

The gene encoding a short-chain alcohol dehydrogenase, AdhA, has been identified in the hyperthermophilic archaeon Pyrococcus furiosus, as part of an operon that encodes two glycosyl hydrolases, the beta-glucosidase CelB and the endoglucanase LamA. The adhA gene was functionally expressed in Escherichia coli, and AdhA was subsequently purified to homogeneity. The quaternary structure of AdhA is a dimer of identical 26-kDa subunits. AdhA is an NADPH-dependent oxidoreductase that converts alcohols to the corresponding aldehydes/ketones and vice versa, with a rather broad substrate specificity. Maximal specific activities were observed with 2-pentanol (46 U x mg(-1)) and pyruvaldehyde (32 U x mg(-1)) in the oxidative and reductive reaction, respectively. AdhA has an optimal activity at 90 degrees C, at which temperature it has a half life of 22.5 h. The expression of the adhA gene in P. furiosus was demonstrated by activity measurements and immunoblot analysis of cell extracts. A role of this novel type of archaeal alcohol dehydrogenase in carbohydrate fermentation is discussed.
 ...
PMID:Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. 1135 25

To determine the liquid culture conditions under which the wood-degrading system of the brown-rot fungus Gloeophyllum trabeum is expressed, enzymes and metabolites from liquid and solid substrate cultures were characterized. Enzymes were analyzed by 2-D gel electrophoresis and also assayed. Growth conditions were varied by using liquid media containing: (1) low carbon, low nitrogen, (2) low carbon, high nitrogen, (3) high carbon, low nitrogen, or (4) high carbon, high nitrogen. The protein arrays expressed under the four conditions were very similar, and endo-1,4-beta-glucanase (detected by 2-D gels) activity along with beta-glucosidase, xylanase, and NADH/quinone oxidoreductase activities were detected. Maximal expression of the hydrolytic enzymes was observed in high carbon/high nitrogen medium, whereas the highest oxidoreductase activity was in the high carbon low nitrogen medium. Oxalate and 2,5-dimethoxybenzoquinone were detected under all culture conditions, with higher production in high carbon/low nitrogen medium. Cultures grown in this medium also yielded the highest rate of hydroxylation of p-hydroxybenzoic acid, yielding protocatechuic acid, a product of hydroxyl radical attack.
 ...
PMID:Culture conditions affecting biodegradation components of the brown-rot fungus Gloeophyllum trabeum. 1292 May 6