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 exudates or liquid droplets on various structures of a number of fungi were examined. The droplets were enveloped in membranous material and were associated with actively growing mycelia, including fruiting structures. Osmium tetroxide vapour-fixed droplets of Claviceps purpurea, Myrothecium roridum, Sclerotinia sclerotiorum, Sclerotium rolfsii, and Thanathephorus cucumeris did not dry to a powder but remained intact as spheres when freeze-dried. Fractured spheres, examined with the scanning electron microscope, showed the presence of a membranous structure similar to that of rapidly frozen colloidal solutions with the ice crystals removed by sublimation. Locules or cavities within the freeze-dried droplets are thought to be due to the entrapment of air when droplets coalesce. Biochemical analyses of the exudates showed that acid phosphatase, beta-glucosidase, acid and alkaline protease. RNase polygalacturonase and cellulase enzymes as well as oxalic acid and ammonia were present.
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PMID:Fungal exudates. 72 49

A new type of glycopeptidase hydrolyzing beta-aspartylglycosylamine linkages was partially purified from almond emulsin by chromatography on Sephadex G-200 and DE 52. The enzyme degraded stem bromelain glycopeptide, Asn-Asn(Man3,Xyl1,Fuc1,GlcNAc2)-Glu-Ser-Ser, to yield equimolar amounts of intact oligosaccharide, peptide (Asn-Asp-Glu-Ser-Ser), and ammonia. The Km value for the stem bromelain glycopeptide was 4 mM, and the optimum pH was 5.2. The enzyme was markedly inhibited by 10 mM Cu2+, Fe3+, and Zn2+. Thiol inhibitors and actinomycete protease inhibitors had no effect. The glycopeptides used as substrates were prepared from stem bromelain, ovalbumin or ovotransferrin. The enzyme hydrolyzed glycopeptides with 3-11 amino acid residues, whereas it did not hydrolyze glycopeptides with 1-2 amino acid residues. Furthermore, Asn-oligosaccharide was not inhibitory to the enzyme.
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PMID:Some characteristics of a new glycopeptidase acting on aspartylglycosylamine linkages. 73 97

Effects of corn fiber residue (5 g/day for 10 days) on fecal weight, moisture, pH, fecal flora, ammonia content, and on the activities of beta-glucuronidase and beta-glucosidase were investigated in six healthy subjects. Corn fiber residue was remnant of hemicellulose extraction from corn fiber by calcium hydroxide. Fecal weight showed a tendency to increase, and fecal pH did not change during corn fiber residue supplementation. No remarkable changes in the fecal flora at the bacterial group level were observed. Fecal ammonia content and beta-glucuronidase activity per gram of wet feces decreased slightly but the daily output did not change. Fecal beta-glucosidase activities per gram of wet feces increased significantly (p less than 0.05) and the daily output also tended to increase during corn fiber residue supplementation.
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PMID:Effect of corn fiber residue supplementation on fecal properties, flora, ammonia, and bacterial enzyme activities in healthy humans. 165 31

Hyperammonemia interferes with normal brain function. The effect of ammonia on free and membrane-bound lysosomal enzymes and on mucopolysaccharide metabolism was studied in cultured rat brain cells (ROC-1, hybridoma between C6-astrocytoma and oligodendrocytes). Intralysosomal ammoniagenesis was achieved from urea by endocytosed Jackbean urease followed by incubation of the cultures with urea. The intralysosomal location of urease was evidenced by the protective effects of leupeptin and urea on the stability of intracellular urease. Ammonia formed from urea resulted in an increased secretion of lysosomal arylsulfatase-A (AS-A), but not of the membrane-bound lysosomal beta-glucosidase into the culture medium, thus intralysosomal AS-A activity decreased. Lysosomal, membrane-bound beta-glucosidase activity increased, presumably due to intralysosomal proteolytic protection following an increased lysosomal pH. Intralysosomal ammoniagenesis temporarily impaired 35SO4-glycosaminoglycan degradation of prelabeled cells. The results support the hypothesis that hyperammonemic states may interfere with lysosomal functions in vivo as well in cultured cells.
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PMID:Intralysosomal generation of ammonia from urea by endocytosed urease results in secretion of free lysosomal arylsulfatase-A and increased activity of membrane-bound beta-glucosidase in cultured brain cells. 168 84

Hydrolysis of p-nitrophenyl-beta-D-glucoside by cytosolic beta-glucosidase proceeds with retention of the anomeric configuration. Whereas inactivation of the enzyme by the glucosidase inhibitor conduritol B epoxide (CBE) was extremely slow (ki(max)/Ki 0.57 M-1 min-1) it reacted 130 times more rapidly with 6-bromo-6-deoxy-CBE (Br-CBE). The beta-glucosidase could be labeled with [3H]Br-CBE; incorporation of 1 mol inhibitor/mol enzyme resulted in complete loss of activity. Most of the bound inhibitor was released after denaturation and treatment with ammonia as (1,3,4/2,5,6)-6-bromocyclohexanepentol, thus demonstrating the formation of an ester bond with an active site carboxylate by trans-diaxial opening of the epoxide ring. It was concluded from the Ki values for the epoxide inhibitors and for coduritol B with the cytosolic enzyme and corresponding data for the lysosomal beta-glucosidase that the unusually low reactivity with CBE and Br-CBE is probably due to the inability of the cytosolic enzyme to effectively donate a proton to the epoxide oxygen. An extremely rapid inactivation of the cytosolic beta-glucosidase was caused by bromoconduritol F ((1,2,4/3)-1-bromo-2,3,4-trihydroxycyclohex-5-ene) with ki(max)/Ki 10(5) M-1 min-1. In contrast with the Br-CBE-inhibited enzyme the beta-glucosidase inhibited by bromoconduritol F was subject to spontaneous reactivation with t1/2 approximately 20 min.
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PMID:Active site directed inhibition of a cytosolic beta-glucosidase from calf liver by bromoconduritol B epoxide and bromoconduritol F. 312 52

1. Male Sprague-Dawley rats were fed on either a purified, fibre-free diet or a diet in which half the maize starch was replaced with uncooked amylomaize or potato starch (equivalent to 100 or 200 g amylase-resistant starch (ARS)/kg diet respectively). Changes in short-chain fatty acids (SCFA), pH, ammonia and a number of bacterial variables in caecal contents were then assessed. 2. Both ARS supplements decreased caecal content pH by approximately 1-2 units, with an associated reduction in ammonia concentration. Potato starch significantly decreased the concentration of SCFA in the hindgut, while amylomaize supplementation increased propionic and butyric acids but decreased the occurrence of minor, branched-chain fatty acids. 3. Caecal bacterial biotransformation activities (beta-glucosidase (EC 3.2.1.21), beta-glucuronidase (EC 3.2.1.31), reduction of p-nitrobenzoic acid, apparent ammonia formation) were consistently decreased by both ARS sources. 4. The results demonstrate that amylase-resistant carbohydrate altered toxicologically important functions in the large-intestinal flora of the rat.
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PMID:Influence of starches of low digestibility on the rat caecal microflora. 321 26

Male Sprague-Dawley rats were fed a purified fibre-free diet containing 5% (w/w) sodium saccharin for 4 weeks or 20 weeks and changes in caecal bacterial numbers and enzyme activities (endogenous ammonia production, beta-glucosidase, beta-glucuronidase, nitrate reductase, nitroreductase, aryl sulphatase) determined in vitro. Saccharin treatment gave marked caecal enlargement but had no effect on bacterial concentration at either treatment period, and significantly decreased beta-glucuronidase, nitrate reductase and sulphatase activities/g caecal contents. The incubation of a suspension of caecal contents from control rats with saccharin (75 mM) in vitro inhibited beta-glucuronidase and nitrate reductase activities, and ammonia production from endogenous substrates. Such changes may decrease the rate of formation of toxic bacterial products in the hindgut.
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PMID:Modification of rat caecal microbial biotransformation activities by dietary saccharin. 384 Feb 94

1. T.l.c. with neutral solvent systems of ethyl anthranilate azopigments derived from bile of man, dog and rat revealed pronounced species variation. The less polar components (alpha-group) could be separated conveniently by development with chloroform-methanol (17:3, v/v). 2. The azopigment material derived from gallbladder bile of dog contained about 10% of azobilirubin beta-d-monoxyloside (azopigment alpha(2)) and 30% of azobilirubin beta-d-monoglucoside (azopigment alpha(3)). The sugar moieties were identified by t.l.c. with acidic, neutral and basic solvent systems and by anion-exchange column chromatography of their boric acid complexes. Treatment of the purified azopigments with ammonia vapour led to the formation of the amide of azobilirubin, indicating that both pigments are ester glycosides. The beta-d configuration was demonstrated by enzymic studies with emulsin (an adequate source of beta-glucosidase activity) and with Mylase-P (an adequate source of beta-glucosidase and beta-xylosidase activities). 3. Hydrolysis studies with model substrates and with the alpha(2)- and alpha(3)-azopigments suggested that in Mylase-P the beta-glucosidase and beta-xylosidase activities reside in separate enzymes. 4. Compared with the accepted conjugation with glucuronic acid as a major route of detoxication in mammals, the detection of large amounts of xylose and glucose conjugates of bilirubin in dog bile suggests that the underlying biosynthetic pathways may be important alternative routes of detoxication.
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PMID:Excretion in dog bile of glucose and xylose conjugates of bilirubin. 514 3

Variations between and within individuals, and correlations between concentrations of bacterial metabolites, including putrefactive products, ammonia and short chain fatty acids (SCFAs), enzyme activities, moisture and pH, as well as bacterial composition, were studied in faecal samples from seven healthy adults over a period of 7 months. Large variations, both between and within individuals, were observed in concentrations of putrefactive products. Although values for ammonia, SCFAs, enzyme activities, moisture and pH were generally variable, significant person-to-person differences were observed. While ranges of log viable counts of the predominant bacteria such as eubacteria, bifidobacteria and bacteroides in each subject remained between 0.2 and 1.3, those of enterobacteria, streptococci (including enterococci) and lecithinase-negative clostridia varied between 0.4 and 3.0. Levels of bifidobacteria, enterobacteria, streptococci and total aerobic bacteria showed inter-individual variations. Correlations were found among certain of the parameters: moisture correlated negatively with p-cresol (r = -0.707), pH (r = -0.671) and beta-glucosidase activity (GS) (r = -0.608), and positively with acetic acid (r = 0.621), while negative correlations were observed in pH with acetic and butyric acids (r = -0.690 and -0.623, respectively). No significant correlations were found between bacterial compositions, and other faecal factors such as pH, moisture, metabolic enzyme activities and concentrations of putrefactive products.
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PMID:Variations in concentrations of bacterial metabolites, enzyme activities, moisture, pH and bacterial composition between and within individuals in faeces of seven healthy adults. 796 Nov 90

The mechanism underlying exhaustive exercise-induced release of lysosomal enzymes was studied in the rat liver. Exhaustive exercise resulted in the release of beta-glucuronidase and cathepsin D, but not beta-glucosidase and acid phosphatase, into the blood and cytosol, suggesting that the release of lysosomal enzymes is not due to disruption of lysosomal membranes. The intralysosomal pH of the liver, which was approximately 5.5 at the resting level, rose significantly after exhaustive exercise to pH 6.3. In vitro, beta-glucuronidase and cathepsin D were released at an intralysosomal pH exceeding 6.2. In contrast, beta-glucosidase and acid phosphatase were not released. The elevation of intralysosomal pH reduced the aggregation of beta-glucuronidase and cathepsin D. The rate of ammonia accumulation increased markedly in the lysosome-enriched subcellular fraction after exercise. There was a positive relationship between the rate of ammonia accumulation and the elevation of intralysosomal pH in vitro. Lysosomes isolated after exhaustive exercise showed significantly increased osmotic fragility. Our findings suggest that, during exhaustive exercise, the accumulation of ammonia in lysosomes leads to the elevation of intralysosomal pH, resulting in the reduced aggregation of certain lysosomal enzymes. Thus, less aggregated lysosomal enzymes may be released into the cytosol through the lysosomal membrane, the permeability of which has been increased.
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PMID:Intralysosomal pH and release of lysosomal enzymes in the rat liver after exhaustive exercise. 851 76


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