Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

1. Tests for glycosidases were performed in homogenates of Brachionus plicatilis. 2. Hydrolytic activity was detected with the following substrates: (a) with synthetic substrates (NP = 4-nitrophenyl): NP-alpha- and NP-beta-D-glucopyranoside, NP-alpha- and NP-beta-D-galactopyranoside, NP-N-acetyl-beta-D-glucosaminide, NP-N-acetyl-beta-D-galactosaminide, NP-alpha- and NP-beta-D-mannopyranoside and NP-alpha-L-fucopyranoside; (b) with disaccharides: sucrose, maltose, trehalose, isomaltose, cellobiose, gentiobiose and lactose; (c) with polysaccharides: laminarine, carboxymethyl-cellulose, avicel, Micrococcus luteus (for lysozyme) and 4-nitrophenyl-alpha-D-maltoheptaoside (for amylase). 3. The pH dependence of the glycosidase activities was determined. 4. The distribution of enzyme activities within fractions from the homogenate was studied in order to localize them within the cell. 5. Proteins from Brachionus homogenate were separated by SDS-gel electrophoresis and the positions of the following glycosidase activities were detected by assays performed on the gels (estimated molecular weights in parentheses): alpha-glucosidase (250,000); beta-glucosidase (200,000); beta-galactosidase (70,000); N-acetyl-beta-glucosaminidase (60,000).
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PMID:Glycosidases in Brachionus plicatilis (Rotifera). 232 73

A beta-glucosidase has been purified to electrophoretically homogeneity from the wheat bran culture of Aspergillus phoenicis by PEG 6000-phosphate biphasic separation, column chromatography on Sephadex G-100, DEAE-Sephadex A-50 and SE-Sephadex C-50. The enzyme showed optimal activity at pH 5.0 and 60 degrees C. It was stable in the pH range of 4.0-7.5 and up to 55 degrees C. The enzyme activity was strongly inhibited by Ag+ and Hg2+. The molecular weight of the enzyme was 118000 as determined by SDS-PAGE and 195000 by gradient-PAGE. The isoelectric point was pI 3.95 as determined by PAGIF.
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PMID:[Purification and properties of beta-glucosidase from Aspergillus phoenicis]. 250

The complete nucleotide sequence of the beta-glucosidase gene of Kluyveromyces fragilis has been determined. This sequence contains an open reading frame of 2535 base pairs encoding a protein of 845 amino acids. Analysis of the transcription products revealed only one transcript of about 3 kb identical in both Kluyveromyces fragilis and in the expression host Saccharomyces cerevisiae. The protein molecular weight of 93,811 Kd deduced from the sequence is consistent with the 90,000 Kd determined by SDS polyacrylamide gel electrophoresis with the purified protein. Mapping of the starts of transcription shows that two starting points are used in the natural host Kluyveromyces fragilis. A comparison of the amino acid sequence with that of other beta-glucosidases revealed three regions of homology. One of these regions contains an amino acid sequence very similar to a peptide isolated from the active site of beta-glucosidase A3 from Aspergillus wentii and could be implicated in the catalytic mechanism of these glucolytic enzymes.
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PMID:Sequence and transcription of the beta-glucosidase gene of Kluyveromyces fragilis cloned in Saccharomyces cerevisiae. 283 79

Extracellular cellulolytic enzymes produced by a species of Monilia could be fractionated by chromatography on SP-Sephadex, Con A-Sepharose, and cellobiose-Sepharose. These methods did not separate the beta-D-glucosidases (beta-D-glucoside glucohydrolases, EC 3.2.1.21) from the cellulases and xylanases within a single purification step. Fractionation by isoelectric focusing on a flat-bed granulated gel gave all of the beta-D-glucosidase activity in a single zone isoelectric at pH 8-9. The beta-D-glucosidase could be further purified to homogeneity by column isoelectric focusing at pH 8.0-10.5, and gel filtration on Biogel P-100. The purified beta-D-glucosidase showed optimal activity at pH 4-5 and 50 degrees, was isoelectric at pH 8.87, and had a molecular weight of 46,600. SDS-Polyacrylamide-gel electrophoresis demonstrated that the beta-D-glucosidase was not dissociated into subunits and, hence, consisted of a single polypeptide chain. The enzyme is considered a glycoprotein, as it binds to Con A-Sepharose. The beta-D-glucosidase hydrolyzed (1----2)-, (1----4)-, and (1----6)-beta-D-glucosidic linkages but not cellulose. Nitrophenyl beta-D-glucopyranosides and beta-D-xylopyranosides were also degraded. The beta-D-glucosidase was competitively inhibited by D-glucose (Ki 0.67 mM).
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PMID:Fractionation of the cellulolytic enzymes produced by a species of Monilia; purification and properties of an extracellular beta-D-glucosidase. 310 61

We have isolated a heat-stable, low molecular weight activator peptide(s) from monkey parotid gland that specifically activated human salivary beta-D-glucosidase. This activator appeared to be heterogeneous on Sephadex G-25 gel filtration and polyacrylamide gel electrophoresis under non-denaturing conditions. About 45% of the human salivary beta-glucosidase could bind to the activator immobilised on Sepharose and be eluted by Cutscum. The purified enzyme was nearly homogeneous, with a subunit Mr of 46,000 as revealed by SDS-gel electrophoresis and silver staining.
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PMID:A heterogeneous beta-D-glucosidase activator from monkey parotid gland and its use as an affinity ligand in the purification of human salivary beta-D-glucosidase. 310 68

A beta-D-glucosidase (linamarase) was purified 11,700-fold from the butter bean, Phaseolus lunatus L., by means of successive procedures including extraction, ammonium sulfate fractionation, acetone treatment, and chromatographies on CM-Sephadex, DEAE-Sephadex, and Sephadex G-200. The final preparation gave a single protein band on both disc polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. In spite of its electrophoretic purity, the final enzyme preparation showed four glycosidase activities; beta-D-glucosidase, beta-D-galactosidase, beta-D-fucosidase, and beta-D-xylosidase. The molecular weight of the enzyme was determined to be 124,000 +/- 9,000 by Sephadex G-200 gel filtration, and 59,000 +/- 2,400 by SDS-disc gel electrophoresis. The enzyme showed a pH optimum in the range of 5.1 to 6.0 with p-nitrophenyl beta-D-glucoside, 4-methylumbelliferyl beta-D-glucoside, and linamarin. Among natural substrates containing a beta-glucosyl terminal, linamarin, prunasin, and salicin were hydrolyzed by the enzyme from butter beans, but amygdalin, cellobiose, gentiobiose, and laminarin were hardly hydrolyzed.
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PMID:Purification and properties of beta-D-glucosidase (linamarase) from the butter bean, Phaseolus lunatus. 311 32

This enzyme shows beta-D-glucosidase, beta-D-fucosidase and beta-D-galactosidase activities, all associated in a single peak in Sephadex G-200, DEAE-cellulose, concanavalin A-Sepharose chromatographies, and in high resolution isoelectric focusing (pI 4.56), having the optimal pH in the range 4.5-5.5. The enzyme is very stable under different conditions: (i) at pH in the range 5.5-7.0; (ii) in successive freezing-thawing cycles; (iii) at 4 degrees C; (iv) after exhaustive ultrasonic treatment. It is not stable beyond 40 degrees C, and in the presence of urea, Triton X-100, SDS or mercaptoethanol. HgCl2, KCN, Tris, maltose and the lactones were inhibitors of the enzyme. With glucose, fucose and galactose the inhibition is competitive. In addition, a transglycosylation mechanism seems to occur. The kinetic studies suggest a substrate-activation model and the presence of two primary active sites: fuco-gluco and galacto.
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PMID:Characterization and kinetics of beta-D-gluco/fuco/galactosidase from sheep liver. 641 26

Polyacrylamide gel electrophoresis of the cellulolytic system from culture supernates of Acetivibrio cellulolyticus showed the presence of four major enzymes: a beta-glucosidase, an exoglucanase, and two endoglucanases. The relative proportions of these enzymes in the culture supernate were affected by the nature of the cellulosic substrate and by the length of the incubation period. The molecular weights of the cellulolytic enzymes were beta-glucosidase, 81 000; exoglucanase, 38 000; endoglucanase C2, 33 000; and endoglucanase C3, 10 400, as estimated by their electrophoretic mobilities relative to proteins of known molecular weight. Treatment of the high molecular weight endoglucanase with SDS--mercaptoethanol led to reversible dissociation of the enzyme into polypeptide subunits similar to the low molecular weight endoglucanase. Endoglucanase activity could be assayed for directly using a novel method of incorporating carboxymethyl cellulose in the polyacrylamide gels. The molecular weights and functions of these enzymes are compared with those detected in culture filtrates of various fungi.
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PMID:Cellulolytic enzyme system of Acetivibrio cellulolyticus. 678 18

beta-D-Mannosidase (beta-D-mannoside mannohydrolase EC 3.2.1.25) was purified 160-fold from crude gut-solution of Helix pomatia by three chromatographic steps and then gave a single protein band (mol. wt. 94,000) on SDS-gel electrophoresis, and three protein bands (of almost identical isoelectric points) on thin-layer isoelectric focusing. Each of these protein bands had enzyme activity. The specific activity of the purified enzyme on p-nitrophenyl beta-D-mannopyranoside was 1694 nkat/mg at 40 degrees and it was devoid of alpha-D-mannosidase, beta-D-galactosidase, 2-acetamido-2-deoxy-D-glucosidase, (1 leads to 4)-beta-D-mannanase, and (1 leads to 4)-beta-D-glucanase activities, almost devoid of alpha-D-galactosidase activity, and contaminated with less than 0.02% of beta-D-glucosidase activity. The purified enzyme had the same Km for borohydride-reduced beta-D-manno-oligosaccharides of d.p. 3-5 (12.5mM). The initial rate of hydrolysis of (1 leads to 4)-linked beta-D-manno-oligosaccharides of d.p. 2-5 and of reduced beta-D-manno-oligosaccharides of d.p. 3-5 was the same, and o-nitrophenyl, methylumbelliferyl, and naphthyl beta-D-mannopyranosides were readily hydrolysed. beta-D-Mannobiose was hydrolysed at a rate approximately 25 times that of 6(1)-alpha-D-galactosyl-beta-D-mannobiose and 6(3)-alpha-D-galactosyl-beta-D-mannotetraose, and at approximately 90 times the rate for beta-D-mannobi-itol.
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PMID:beta-D-Mannosidase from Helix pomatia. 683 86

Previous studies have shown that Biomphalaria glabrata contains a complete cellulolytic system which includes an endoglucanase, an exoglucanase and a beta-glucosidase. In the present report, a scheme for the purification of the endoglucanase from this invertebrate is proposed. Two major problems were encountered during the study: 1) the presence of a green-brownish pigment, which could not be eliminated by thermal shock or ammonium sulfate precipitation and 2) relative instability of enzymatic activity. Various alternatives were tested and the best sequence of steps was: 1) a sample of the crude extract, obtained by homogenization of the digestive glands in 50 mM Tris-HCl buffer, pH 8.4, and ultracentrifugation, was applied to a Q-Sepharose FPLC column (50 mM Tris-HCl buffer, pH 8.4; 10 mm x 22.2 cm column; flow rate 1.5 ml/min; 0.1 to 0.5 M NaCl gradient); 2) the eluate peak containing activity was dialyzed, lyophilized and eluted from a Superdex-75 gel filtration FPLC column (50 mM ammonium acetate buffer, pH 4.8; 16 mm x 60 cm column; flow rate 1.0 ml/min). A low degree of purification (about 36-fold) and recovery (about 12%) were observed, probably due to enzyme instability. SDS-electrophoresis of the active fraction showed a major peak of 30 kDa. In order to improve the purification scheme, further studies are required to stabilize this enzyme during purification and storage.
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PMID:Partial purification of an endoglucanase from Biomphalaria glabrata. 754 74


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