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)

The extracellular cellulase system of the white-rotting basidiomycete Ganoderma lucidum was characterised while growing in cellulose-containing shaken liquid culture. The protein content of the culture filtrate reached its maximum after 36 days and cellulase activity at about 60 days. Different cellulase activities (endoglucanase, cellobiohydrolase and beta-glucosidase) were determined in a range of pH extending from 6 to 2. All of the three enzyme activities have at least three peaks between pH 6 and 2, although optimum points of the different enzymes are slightly different, showing that the enzyme complex consists of a number of enzymes and isozymes. Partial purification of the enzyme complex was carried out by DEAE-cellulose column chromatography. Using 0-3 M linear urea gradient, protein was eluted in one sharp peak corresponding mainly to beta-glucosidase activity. Comparing crude extracellular protein with that of purified by the column using PAGE indicated that this method was suitable for the separation and partial purification of one type of Ganoderma cellulases.
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PMID:Some characteristics and partial purification of the Ganoderma lucidum cellulase system. 792 48

Mutations enhancing the thermostability of beta-glucosidase A of Bacillus polymyxa, a family 1 glycosyl hydrolase, have been obtained after hydroxylamine mutagenesis of a plasmid containing the bglA gene, transformation of Escherichia coli with the mutagenized plasmid, and identification of transformant colonies that showed beta-glucosidase activity after a thermal treatment that inactivated the wild-type enzyme. Two additive mutations have been characterized that cause replacement of glutamate at position 96 by lysine and of methionine at position 416 by isoleucine respectively. The thermoresistant mutant enzymes showed increased resistance to other denaturing agents, such as pH and urea, while their kinetic parameters did not change. CD spectra indicated that the E96K replacement caused an increase in alpha-helix content. The observed effect of the M416I mutation is consistent with the lower content of cysteine and methionine found in family 1 enzymes of thermophilic species compared with similar ones from mesophilic organisms.
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PMID:Amino acid substitutions enhancing thermostability of Bacillus polymyxa beta-glucosidase A. 861 77

The removal of noncovalently bound polysaccharide coating from the extracellular enzymes of Aspergillus niger, by the technique of compartmental electrophoresis, had a very dramatic effect on the stability of beta-glucosidase. The polysaccharide-beta-glucosidase complex was extremely resistant to proteinases and far more stable against urea and temperature as compared with polysaccharide-free beta-glucosidase. The beta-glucosidase-polysaccharide complex was 18-, 36-, 40- and 82-fold more stable against chymotrypsin, 3 mol/L urea, total thermal denaturation and irreversible thermal denaturation, respectively, as compared with polysaccharide-free beta-glucosidase. The activation energy of polysaccharide-complexed beta-glucosidase (55 kJ/mol) was lower than polysaccharide-free enzyme (61 kJ/mol), indicating a slight activation of the enzyme by the polysaccharide. No significant difference could be detected in the specificity constant (V/K(m)) for A-nitrophenyl beta-D-glucopyranoside between polysaccharide-free and polysaccharide-complexed beta-glucosidase. We suggest that the function of these polysaccharides secreted by fungi including A. niger might be to protect the extracellular enzymes from proteolytic degradation, hence increasing their life span.
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PMID:The stability of extracellular beta-glucosidase from Aspergillus niger is significantly enhanced by non-covalently attached polysaccharides. 913 91

The high-molar mass form of beta-glucosidase from Aspergillus niger strain NIAB280 was purified to homogeneity with a 46-fold increase in purification by a combination of ammonium sulfate precipitation, hydrophobic interaction, ion-exchange and gel-filtration chromatography. The native and subunit molar mass was 330 and 110 kDa, respectively. The pH and temperature optima were 4.6-5.3 and 70 degrees C, respectively. The K(m) and kcat for 4-nitrophenyl beta-D-glucopyranoside at 40 degrees C and pH 5 were 1.11 mmol/L and 4000/min, respectively. The enzyme was activated by low and inhibited by high concentrations of NaCl. Ammonium sulfate inhibited the enzyme. Thermolysin periodically inhibited and activated the enzyme during the course of reaction and after 150 min of proteinase treatment only 10% activity was lost with concomitant degradation of the enzyme into ten low-molar-mass active bands. When subjected to 0-9 mol/L transverse urea-gradient-PAGE for 105 min at 12 degrees C, the nonpurified beta-glucosidase showed two major bands which denatured at 4 and 8 mol/L urea, respectively, with half-lives of 73 min.
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PMID:Purification and characterization of a beta-glucosidase from Aspergillus niger. 943 54

The effect of Bifidobacterium longum (4 x 10(8) viable cells/g diet) and a derivative of inulin ('Raftiline HP'; 5% w/w in diet) on colonic aberrant crypt foci (ACF) induced by the colon carcinogen azoxymethane (AOM) has been studied. The concentration of ammonia, a putative tumour promoter produced by bacterial degradation of protein and urea, and the activities of certain bacterial enzymes thought to play a role in colon carcinogenesis, beta-glucuronidase and beta-glucosidase were also assayed. Consumption of either B. longum or inulin was associated with a decrease (26 and 41%, respectively) in AOM-induced small ACF (i.e. those comprising 1-3 aberrant crypts per focus). Combined administration of the bifidobacterium and inulin resulted in more potent inhibition of ACF than administration of the two separately, achieving 80% inhibition of small ACF. Furthermore, the combined administration significantly decreased the incidence (by 59%) of large ACF (>4 aberrant crypts per focus), which are considered to be predictive of eventual tumour incidence. Since the dietary treatments were started 1 week after the carcinogen dose, the results suggest that B. longum and inulin may be affecting the early promotion phase of the carcinogenic process. Consumption of diets containing B. longum, inulin or both were also associated with decreases in beta-glucuronidase activity and ammonia concentration in the caecal contents. Both these factors have been associated with carcinogenesis of the colon in experimental animal models. In rats given inulin-containing diets (with or without B. longum) an increase in caecal wt and beta-glucosidase activity and a decrease in caecal pH were observed. The results suggest that consumption of B. longum or inulin was associated with potentially beneficial changes in caecal physiology and bacterial metabolic activity in relation to tumour risk and in the incidence of putative preneoplastic lesions in the colon. The results also indicated that combined treatment with the two agents was more effective in reducing colonic lesions.
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PMID:Effect of Bifidobacterium longum and inulin on gut bacterial metabolism and carcinogen-induced aberrant crypt foci in rats. 949 77

The production of the extracellular cellulolytic enzyme system (endoglucanase, exoglucanase and cellobiase) of N. catalinensis was tested with different nitrogen sources, inorganic and organic ones, in liquid culture medium with microcrystalline cellulose. The nitrogen compounds used were: potassium nitrate, sodium nitrate, ammonium nitrate, ammonium phosphate, ammonium sulphate, ammonium chloride, ammonium carbonate, ammonium acetate, ammonium tartrate, urea, casamino acids, glycine, L-alanine, L-leucine, L-proline, L-lysine, L-aspartic acid, L-glutamic acid, L-asparagine, L-glutamine, L-phenylalanine, L-tyrosine, L-tryptophan, L-methionine and L-cysteine. Among these, ammonium nitrate and ammonium tartrate gave the highest yields of cellulases in 20-day-old cultures at a concentration equivalent to 0.75 g N/l in both cases. Optimal temperature for cellulase production, growth and cellulose degradation was 23 degrees C. On the other hand, an initial pH of 6.5 gave the highest yields of endoglucanase and cellobiase. In the same way, at pH 6.5, maximal growth and cellulose degradation were achieved. However, maximal exoglucanase production and glycogen content were reached at pH 7.5.
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PMID:Influence of different cultural conditions on cellulase production by Nectria catalinensis. 962 4

Oat beta-glucosidase (EC 3.2.1.21) has two isomeric forms, type I and type II, which are composed of 60 kDa peptides. To study the subunit composition and the stability of multimeric structure, the type I and II were purified from the primary leaves and coleoptiles of the etiolated oat seedlings where the isozymes are expressed organ-specifically. The monomers of the isozymes were isolated by urea-denatured gel electrophoresis followed by electroblotting. N-Terminal amino acid sequencing of the monomers indicated that the type I consisted of a peptide of ALESAKQVKPWQVPKRDWFP (As-Glu 1), and the type II having a peptide of ALESGKLKPWQIPKRDWFP (As-Glu 2) and As-Glu 1 in 1:1 ratio. The C-terminal amino acid of the As-Glu 1 was alanine and that of the As-Glu 2 was lysine. The As-Glu 2 was more negatively charged than the As-Glu 1. The type I isozyme is thus homomultimer of As-Glu 1 monomer and the type II heteromultimer of As-Glu 1 and As-Glu 2 monomers in 1:1 ratio. Partial denaturation of the multimers with urea and CaCl2 broke down the higher multimers to the lower multimers, which were in turn dissociated into homodimers and heterodimer. Denaturation study with urea and CaCl2 indicate that the higher multimers of the homooligomeric type I were more stable than those of the heterooligomeric type II and that hydrophobic interactions were important in the multimer formation. The homodimers were found to be more stable than the heterodimer. These results indicate that different combinations of the As-Glu 1 and As-Glu 2 monomers form the two isozymes of oat beta-glucosidase with different enzymatic properties and structural stability.
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PMID:Subunit composition and oligomer stability of oat beta-glucosidase isozymes. 985 80

To determine whether there are early renal function parameters (RFP) which can be monitored to rapidly detect nephrotoxicity induced by contrast media (CM), we observed RFP in 16 patients with normal renal function before and after administration of CM. Forty-eight hours after diatrizoate meglumine administration, blood urea nitrogen (BUN) and serum creatinine (SCr) increased (p < 0.05). In all patients, acute tubular damage was revealed by early urinary RFP. Increases in levels of serum angiotensin-I-converting enzyme (ACE), beta(2)-microglobulin (beta(2)M) and urinary albumin (Alb) were associated with alterations in glomerular function. The changes in early RFP occurred earlier than those of BUN and SCr. The present study demonstrates that serum ACE, beta(2)M, urinary Alb, gamma-glutamyl-transpeptidase and N-acetyl-beta-D-glucosidase are sensitive parameters for the early assessment of subclinical nephrotoxicity induced by CM.
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PMID:Assessment of renal function in the early stages of nephrotoxicity induced by iodinated contrast media. 1051 90

The maize Zm-p60.1 gene encodes a beta-glucosidase that can release active cytokinins from their storage forms, cytokinin-O-glucosides. Mature catalytically active Zm-p60.1 is a homodimer containing five cysteine residues per a subunit. Their role was studied by mutating them to alanine (A), serine (S), arginine (R) or aspartic acid (D) using site-directed mutagenesis, and subsequent heterologous expression in Escherichia coli. All substitutions of C205 and C211 resulted in decreased formation and/or stability of the homodimer, manifested as accumulation of high levels of monomer in the bacterial expression system. Examination of urea- and glutathione-induced dissociation patterns of the homodimer to the monomers, HPLC profiles of hydrolytic fragments of reduced and oxidized forms, and a homology-based three-dimensional structural model revealed that an intramolecular disulfide bridge formed between C205 and C211 within the subunits stabilized the quaternary structure of the enzyme. Mutating C52 to R produced a monomeric enzyme protein, too. No detectable effects on homodimer formation were apparent in C170 and C479 mutants. Given the Km values for C170A/S mutants were equal to that for the wild-type enzyme, C170 cannot participate in enzyme-substrate interactions. Possible indirect effects of C170A/S mutations on catalytic activity of the enzyme were inferred from slight decreases in the apparent catalytic activity, k'cat. C170 is located on a hydrophobic side of an alpha-helix packed against hydrophobic amino-acid residues of beta-strand 4, indicating participation of C170 in stabilization of a (beta/alpha)8 barrel structure in the enzyme. In C479A/D/R/S mutants, Km and k'cat were influenced more significantly suggesting a role for C479 in enzyme catalytic action.
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PMID:The role of cysteine residues in structure and enzyme activity of a maize beta-glucosidase. 1058 2

We have isolated 5 cDNA clones (din2, din6, din9, din10 and din11) corresponding to genes, the transcripts of which accumulated in leaves of Arabidopsis thaliana kept in the dark. These cDNA clones encode proteins similar to beta-glucosidase (EC 3.2.1.21, din2), asparagine synthetase (EC 6.3.5.4, din6), phosphomannose isomerase (EC 5.3.1.8, din9), seed imbibition protein (din10) and 2-oxoacid-dependent dioxygenases (din11). Accumulation of the transcripts from din6 and din10 occurred within 3 h after plants were transferred to darkness. The transcripts from din2, din9 and din11 were only detected after 24 h of dark treatment. We also observed the accumulation of the din transcripts in senescing leaves. Application of a photosynthesis inhibitor, 3-(3,4-dichlorophenyl)-1-1-dimethyl-urea, induced the expression of the din genes under illumination. Application of sucrose to detached leaves suppressed the accumulation of the din transcripts in the dark. These results indicate that expression of these genes partly depends on cellular sugar level. The sugar-modulated expression of the din genes suggests that dark-induced expression of these genes might be related to sugar starvation occurring in leaf cells in the dark, when the photosynthesis is hindered.
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PMID:Dark-inducible genes from Arabidopsis thaliana are associated with leaf senescence and repressed by sugars. 1124 Sep 19


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