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

A Streptomyces sp. isolated from compost degraded the hemicellulose fraction of straw efficiently but apparently not native cellulose. Ball-milled straw induced endoglucanase, beta-glucosidase, beta-xylanase and beta-xylosidase. Carboxymethylcellulose, cellotetraose and cellotriose induced cellulolytic enzymes specifically whereas cellobiose acted as inducer for beta-glucosidase only. Cellotriose and cellotetraose induced beta-glucosidase, but only partially induced endoglucanase. Hemicellulose (in the form of xylan) and xylobiose induced only beta-xylanase and beta-xylosidase. Kraft lignin and syringic acid induced beta-xylanase and endoglucanase but not the other enzymes. 3,4-Dimethoxycinnamic acid slightly induced beta-xylanase whereas 3,5-dimethoxy-4-hydroxycinnamic acid specifically induced endoglucanase. Neither veratric acid nor vanillic and ferulic acids induced any of the cellulolytic or hemicellulolytic enzymes. Enzyme production was subject to a form of carbon catabolite repression. Endoglucanase and beta-xylanase were excreted into the culture medium. Four protein components, one acidic (pI 5.2) and three basic (pI 8.15, 8.45 and 8.65) exhibited beta-xylanase activity. Two acidic components (pI 3.55 and 3.75) displayed endoglucanase activity.
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PMID:Regulation of the production of hemicellulolytic and cellulolytic enzymes by a Streptomyces sp. growing on lignocellulose. 251 44

trans-p-Coumaric acid inhibited the growth of Bacteroides ruminicola on both cellobiose and glucose, while trans-ferulic acid and vanillin retarded growth. The phenolic monomers varied in their potential to inhibit the Bacteroides succinogenes beta-glucosidase, carboxymethylcellulase, and xylanase, with p-coumaric acid being the most inhibitory. The B. ruminicola beta-glucosidase was inhibited less than 10% by all three compounds.
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PMID:Effect of phenolic monomers on the growth and beta-glucosidase activity of Bacteroides ruminicola and on the carboxymethylcellulase, beta-glucosidase, and xylanase activities of Bacteroides succinogenes. 314 48

During cell-free experiments with membranes isolated from carnation petals (Dianthus caryophillus L. cv White Sim), the conversion of 1-aminocyclopropane-1-carboxylic acid into ethylene was blocked by a factor derived from the cytosol. Subsequent characterization of the inhibitor revealed that its effect was concentration dependent, that it was water soluble, and that it could be removed from solution by dialysis and addition of polyvinyl-polypyrrolidone. Activity profiles obtained after solvent partitioning over a range of pH values and after chromatography on silica gel, size exclusion gel, and ion exchange resins revealed that the inhibitor was a highly polar, low molecular weight species that was nonionic at low pH and anionic at pH values above 8. Use of selected solvent systems during paper and thin layer chromatography combined with specific spray reagents tentatively identified the compound as a hydroxycinnamic acid derivative. Base hydrolysis and subsequent comparison with known standards by high performance liquid chromatography, gas-liquid chromatography, and ultraviolet light spectroscopy established that the inhibitor was a conjugate with a ferulic acid moiety. Release of ferulic acid following treatment with beta-glucosidase also indicated the presence of a glucose moiety, and unequivocal identification of the inhibitor as 1-O-feruloyl-beta-d-glucose was confirmed by gas chromatography-mass spectroscopy and by ultraviolet light, (1)H-, and (13)C- nuclear magnetic resonance spectroscopy. Feruloylglucose constituted about 0.1% of the dry weight of stage III (preclimacteric) carnation petals, but concentrations fell sharply during stage IV (climacteric), when ethylene production peaks and the flowers senesce. In a reaction mixture containing microsome-bound ethylene forming enzyme system, 98% of all ethylene production was abolished in the presence of 50 mum concentrations of the inhibitor.
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PMID:Identification of a naturally occurring inhibitor of the conversion of 1-aminocyclopropane-1-carboxylic Acid to ethylene by carnation microsomes. 1666 63