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)

The specific activities of several glycosidases (beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase) were determined in human sera from a control group to 10 normal subjects and in four groups, each of 10 patients, with acute viral hepatitis, acute pancreatitis, acute myocardial infarction and breast cancer. The results show significantly higher activities in acute viral hepatitis for beta-N-acetylglucosaminidase, beta-D-glucosidase and alpha-D-glucosidase (p less than 0.001); in acute pancreatitis for the first two of these enzymes (p less than 0.001); and in breast cancer for beta-D-glucosidase (p less than 0.001). Further, lower differences were found in the patients with acute viral hepatitis for beta-D-fucosidase and alpha-L-fucosidase (p less than 0.01); in acute myocardial infarction for beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase and beta-D-galactosidase (p less than 0.01, p less than 0.05, p less than 0.05, p less than 0.01 and p less than 0.01, respectively); and in breast cancer for beta-N-acetylglucosaminidase (p less than 0.01). No significant differences were found for the other glycosidases.
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PMID:Serum beta-N-acetylglucosaminidase, beta-D-glucosidase, alpha-D-glucosidase, beta-D-fucosidase, alpha-L-fucosidase and beta-D-galactosidase levels in acute viral hepatitis, pancreatitis, myocardial infarction and breast cancer. 680 Jun 74

beta-Galactosidase and associated activities (beta-glucosidase and beta-fucosidase) have been studied in rabbit and bovine liver and rabbit spleen. The physico-chemical (optimal pH, pI, MW) and kinetical (Km, Vmax, Ki) properties were determined for all the activities. Two enzyme forms were separated in rabbit spleen. beta-Galactosidase, beta-fucosidase and beta-glucosidase activities were catalyzed by the same enzyme in rabbit and bovine liver. The enzyme from bovine liver showed nonlinear double-reciprocal plots, suggesting a substrate-activation model, and the presence of more than one binding site in the enzyme. The enzyme activities of several glycosidases were determined in human sera fom control groups and from patients with diabetes mellitus, pancreatitis, hepatitis, cirrhosis, stomach and breast cancer, myocardial infarction and renal failure. The results show significantly different enzyme levels for several glycosidases in all the studied diseases. Experimentally-induced diabetes mellitus, alcoholism and nephrotoxicity in rats showed different glycosidase levels in several tissues, as compared with control groups.
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PMID:[Glycosidases of mammals: association of activities and changes of levels in some disorders]. 681 36

1. The kinetics of beta-D-fucosidase of the snail H. ericetorum have been studied. The enzyme shows beta-D-fucosidase, beta-D-glucosidase and beta-D-galactosidase activities, all associated in a single peak in both DEAE-cellulose chromatography and isoelectric focusing (p1 4.35), having the same optimal pH (5.0). 2. With the corresponding p-nitrophenyl glycosides as substrates, beta-D-fucosidase activity shows the lowest Km, the highest Vmax and the best Vmax/Km value; close activity values were obtained for beta-D-glucosidase, however, beta-D-galactosidase activity is much lower in this enzyme. 3. All the kinetic evidence suggests that this enzyme has two active sites: a fuco-gluco site and a galacto site. 4. beta-D-fucosidase and beta-D-glucosidase activities have similar Km, Vmax, Vmax/Km and Ki values; these values are very different from those of beta-D-galactosidase activity. beta-D-fucosides and beta-D-glucosides completely compete for a common active site in mixed-substrate experiments, while beta-D-galactosides only partially compete with both glycosides. 5. With delta-D-gluconolactone, the enzyme shows a hyperbolic mixed-type inhibition, mainly competitive for beta-D-fucosidase and beta-D-glucosidase activities (with the same inhibition sub-type), and predominantly non-competitive for beta-D-galactosidase activity (with different inhibition sub-type). With delta-D-gluconolactone more inhibition of beta-D-fucosidase and beta-D-glucosidase activities was found, and with gamma-D-galactonolactone, more inhibition of beta-D-galactosidase activity was detected. 6. The enzyme is activated by some carbohydrates, probably in relation with a transglycosylation mechanism.
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PMID:Kinetic evidence for two active sites in beta-D-fucosidase of Helicella ericetorum. 686 81

Homogenates of liver from cases of hepatic cirrhosis due to alpha 1-antitrypsin deficiency (PiZZ) alcoholism were analyzed for their content of various lysosomal enzymes. Also determined were the specific activities of lactate dehydrogenase, glutamate-oxaloacetate transaminase, glutamate-pyruvate transaminase, and creatine phosphokinase in the extracts of liver from cases of both kinds of hepatic cirrhosis: all of these activities were within the range of control values. Similarly, the specific activities of the following lysosomal hydrolases were unremarkable: acid phosphatase, beta-mannosidase, beta-fucosidase, beta-glucuronidase and beta-glucosidase. Hexosaminidase specific activity was increased twofold in livers from the cases of cirrhosis due to alpha 1-antitrypsin deficiency. The specific activity of alpha-mannosidase (measured at pH 4.5) in homogenates of livers from PiZZ individuals with cirrhosis and those with alcoholic cirrhosis was increased two- to four-fold. Chromatography of the high-speed supernatant fraction from homogenates of livers of cirrhotic and noncirrhotic individuals on columns of DEAE-cellulose resolved alpha-mannosidase activity into two components: under the conditions employed, acid pH optimum (pH 4.5) alpha-mannosidase did not bind to the resin, whereas intermediate pH optimum (pH 5.5) alpha-mannosidase could be eluted with 0.1 mol/l NaCl. Liver from one case of (PiZZ) alpha 1-antitrypsin deficiency and emphysema, without demonstrable cirrhosis, was found to contain normal levels of both acid alpha-mannosidase and intermediate alpha-mannosidase. However, cases of cirrhosis due to alpha 1-antitrypsin deficiency contained twice as much acid alpha-mannosidase and only one third to one fourth as much intermediate alpha-mannosidase as controls. The deficiency in hepatic intermediate alpha-mannosidase was also observed in 5 of 5 cases of alcoholic cirrhosis.
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PMID:Altered alpha-mannosidase isoenzymes in the liver in hepatic cirrhosis. 697 51

The importance of bacterial vaginosis as a risk factor in obstetric and gynecological infections has recently been recognized. The bacterial vaginosis group of organisms includes members of the Streptococcus milleri group, the identification of which has caused much confusion. We prospectively surveyed the rates of carriage of S. milleri group organisms in 397 high vaginal swabs received in our laboratory. For the identification of 99 clinical isolates and 23 control strains, we compared the results obtained by the rapid ID 32 Strep system (Analytab Products) and by a scheme utilizing six differential phenotypic characteristics (presence of beta-N-acetylglucosaminidase, alpha-glucosidase, beta-D-fucosidase, beta-galactosidase, beta-N-acetylgalactosaminidase, and beta-glucosidase) as described by Whiley et al. (R. A. Whiley, H. Fraser, J. M. Hardie, and D. Beighton, J. Clin. Microbiol. 28:1497-1501, 1990). We identified Streptococcus anginosus in 18% and Streptococcus constellatus in 0.05% of the specimens examined. Of the isolates of S. anginosus that reacted with grouping antisera, 20 of 25 belonged to Lancefield group F. The incubation conditions for bacterial cultures and for reaction mixtures affected the results of phenotypic characterization in the production of alpha-glucosidase, beta-galactosidase, and beta-glucosidase. However, by using bacterial cultures grown under hypercapnic conditions and incubating the reaction mixtures aerobically, consistent phenotypic characteristics were obtained, allowing identification similar to that obtained by the ID 32 Strep system. We therefore recommend the phenotypic scheme as an inexpensive, reliable, and convenient method for the initial identification of species of the S. milleri group.
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PMID:Species identification of members of the Streptococcus milleri group isolated from the vagina by ID 32 Strep system and differential phenotypic characteristics. 765 Jan 93

Members of the Streptococcus sanguis group (SSG) and Streptococcus milleri group (SMG) were screened for their ability to produce glycosidase, arylamidase (peptidase), protease, dextranase and glycosyltransferase activities. Species within each group produced unique patterns of activity. The most commonly produced glycosidases were beta-D-glucosidase, beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase and the least commonly produced glycosidase activity was beta-fucosidase with Streptococcus intermedius (SMG) being the only species capable of producing the activity. For arylamidase activity, the most commonly produced type was lysine-arylamidase. Glycosidase and arylamidase activities were localized to particular sub-cellular fractions. alpha-galactosidase was found only in culture supernatant fluids whereas N-acetyl-beta-D-glucosaminidase was found in all fractions; the culture supernatant, cell wall, cell membrane and cytoplasm. No arylamidase activity was seen in culture supernatants. Phe-arg-arylamidase was found only in cytoplasmic fractions whereas val-pro-argarylamidase was found in cell walls, cell membranes and cytoplasmic fraction. Protease activity was measured as the degradation of bovine serum albumin (BSA) and casein. Casein was degraded by a number of strains whereas no species/strains were able to degrade BSA. Streptococcus intermedius, Streptococcus constellatus (SMG), Streptococcus mitior and Streptococcus defectivus (SSG) were the only species that produced hyaluronidase and no species produced chondroitin sulphatase. The groups were also examined for their abilities to produce glycosyltransferase and dextranase. Strep. sanguis, Streptococcus gordonii, Streptococcus mitis and Streptococcus oralis produced glucosyltransferase and, with the exception of the latter species, fructosyltransferase. No species within the SMG was capable of producing either glycosyltransferase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Degradative enzymes of oral streptococci. 778 31

Different surveys have been carried out on the plasma activities of different glycosidases in patients with insulin-dependent diabetes mellitus, but research on urinary glycosidases in this disease is scanty and incomplete. To elucidate the behavior of these lysosomal enzymes in the metabolic alterations occurring in the glomerular basal membrane during the initial stages of diabetic nephropathy, we conducted a prospective study to examine the urinary activities of N-acetyl-beta-D-glucosaminidase (NAG), alpha-D-mannosidase, alpha- and beta-D-glucosidase, alpha-L- and beta-D-fucosidase, and beta-D-galactosidase in patients with type I insulin-dependent diabetes mellitus, surveyed over 18 months, whose early diabetic nephropathy was detected by the presence of microalbuminuria. The simultaneous determination of beta 2-microglobulin in urine confirmed the glomerular origin of the albuminuria. No statistically significant correlation was found between the levels of albuminuria and the activities of any of the glycosidases analyzed. In the diabetic patients, a significant decrease was observed in the activities of all the enzymes (p < 0.05), except NAG and alpha-D-mannosidase, although the decrease in the latter was very close to statistical significance (p = 0.028, unilateral; p = 0.057 bilateral). Similarly, in the patients, there was a significant negative correlation (p < 0.05) with the serum levels of fructosamine, except with beta-D-galactosidase, which showed a positive correlation (p < 0.05) with fructosamine and blood HbA1c.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Prospective study of the enzymatic activities in urine of N-acetyl-beta-D-glucosaminidase, alpha-D-mannosidase, alpha- and beta-D-glucosidases, alpha-L- and beta-D-fucosidases, and beta-D-galactosidase in type I diabetes mellitus with early nephropathy. 834 14

A glycosidase enzyme with both beta-glucosidase and beta-fucosidase activities has been purified from the seeds of Dalbergia cochinchinensis Pierre (Thai Rosewood) by ammonium sulfate fractionation, preparative isoelectric focusing, and Sephadex G-150 chromatography. The enzyme has molecular weights of 330,000 in the native state and 66,000 in the denatured state. Hydrolysis of p-NP-beta-D-glucoside and p-NP-beta-D -fucoside showed pH optimum at pH 5.0 and was inhibited by delta-gluconolactone, HgCl2, and p-chloromercuribenzoate. The Km and kcat values of the purified enzyme were 5.4 mM and 307 s-1 for p-NP-beta-D-glucoside and 0.54 mM and 151 s-1 for p-NP-beta-D-fucoside, so that the latter had by far the higher kcat/Km ratio. p-NP-beta-D-galactoside, p-NP-beta-D-xyloside, and p-NP-alpha-L-arabinoside were hydrolyzed more slowly. Hydrolysis of sophorose, laminaribiose, and gentiobiose were also rather slow, and hydrolysis of cellobiose was even slower. No hydrolysis of the cyanogenic glucosides linamarin or prunasin, but some hydrolysis of amygdalin and salicin was found. Further studies are required to identify the natural substrates of the enzyme. However, high yields, ease of purification, and storage stability of the enzyme make it a useful candidate for various applications, such as study of oligosaccharide synthesis by reversal of hydrolysis.
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PMID:Isolation and characterization of an enzyme with beta-glucosidase and beta-fucosidase activities from Dalbergia cochinchinensis Pierre. 883 58

The rumen anaerobic fungus Caecomyces communis was grown in a fermentor in Lowe medium. We studied four polysaccharide hydrolases and three glycoside hydrolases at early and final stages. We found a difference in cell association for these enzymes depending on the developmental stage. The endocellulase and beta-D-fucosidase were early synthesized, and their activities decreased at the end of the developmental cycle. On the contrary, the beta-D-glucosidase, beta-D-xylosidase and xylanase activities increased during the cycle. The avicelase and the CM-cellulase activities linked with thalli increased, whereas the extracellular activities of these enzymes decreased.
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PMID:Glycoside and polysaccharide hydrolase activity of the rumen anaerobic fungus Caecomyces communis (Sphaeromonas communis SENSU ORPIN) at early and final stages of the developmental cycle. 885 72

Genomic DNA encoding a beta-D-glucosidase (EC 3.2.1.21), which has beta-D-fucosidase activity, was cloned from Bifidobacterium breve clb. We sequenced a 1.9-kbp cloned DNA fragment that contained a single open reading frame encoding 460 amino acids with a calculated molecular mass of 51,513 Da. A putative ribosome binding site was found 5 bp upstream of the initiation codon. The amino acid sequence of this beta-D-glucosidase from Bifidobacterium breve clb had 46% identity with that of beta-glucosidase from Microbispore bispore. The enzyme of Bifidobacterium breve clb was expressed in Escherichia coli. A cell-free extract prepared from the recombinant strain showed 80 to 90-fold more beta-D-glucosidase activity than that from Bifidobacterium breve clb. The recombinant enzyme was purified to homogeneity from cell-free extracts of the recombinant strain using 4 column chromatographies. The recovery of enzyme from the recombinant strain was about 138-fold-higher than that of Bifidobacterium breve clb. The enzymatic properties were similar to those of Bifidobacterium breve clb. For application of this recombinant enzyme, we attempted to synthesize a disaccharide that seemed to be specifically assimilated by Bifidobacteria using the condensation activity of the enzyme.
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PMID:Cloning and nucleotide sequence of the beta-D-glucosidase gene from Bifidobacterium breve clb, and expression of beta-D-glucosidase activity in Escherichia coli. 898 33


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