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

---

Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The beta-galactosidase-encoding mbgA gene has recently been cloned from Bacillus megaterium. We now report that disruption of the chromosomal mbgA rendered B. megaterium unable to utilize lactose as a sole carbon source. Complementation of the mbgA mutant with a multicopy plasmid carrying intact mbga restored the ability to utilize lactose for cell growth. Crude extracts from the wild-type B. megaterium cells grown in the presence of lactose exhibited a significant level of lactose-hydrolyzing activity, whereas no activity was observed in crude extracts of the mbgA mutant grown under the same condition. The mbgA gene could also confer the ability of lactose utilization on a lacZ deletion mutant of Escherichia coli. Lactose-hydrolyzing activity was also observed in crude extracts of the lacZ deletion mutant carrying mbgA on a multicopy plasmid. In addition, inactivation of the chromosomal mbgA did not affect lactose induction of expression of the mbgA promoter-xylE transcriptional fusion. Taken together, these results suggest that mbgA is essential for lactose utilization by B. megaterium, but is not involved in generation of the intracellular inducer for lactose induction of mbgA expression.
...
PMID:mbgA-dependent lactose utilization by Bacillus megaterium. 1181 53

The nucleotide sequences of the Lactobacillus helveticus lactose utilization genes were determined, and these genes were located and oriented relative to one another. The lacLM genes (encoding the beta-galactosidase protein) were in a divergent orientation compared to lacR (regulatory gene) and lacS (lactose transporter). Downstream from lacM was an open reading frame (galE) encoding a UDP-galactose 4 epimerase, and the open reading frame had the same orientation as lacM. The lacR gene was separated from the downstream lacS gene by 2.0 kb of DNA containing several open reading frames that were derived from fragmentation of another permease gene (lacS'). Northern blot analysis revealed that lacL, lacM, and galE made up an operon that was transcribed in the presence of lactose from an upstream lacL promoter. The inducible genes lacL and lacM were regulated at the transcriptional level by the LacR repressor. In the presence of glucose and galactose galE was transcribed from its promoter, suggesting that the corresponding enzyme can be expressed constitutively. Lactose transport was inducible by addition of lactose to the growth medium.
...
PMID:Unusual organization for lactose and galactose gene clusters in Lactobacillus helveticus. 1278 21

1. An experimental system suitable for the study of enzyme formation has been described. 2. The formation of beta-galastosidase in E. coli B could be induced by lactose, melibiose, D-galactose and beta-methyl-D-galactoside. 3. Lactose-induced beta-galactosidase formation was found to be inhibited by D-glucose, D-mannose, D-fructose, D-arabinose, and raffinose. 4. The utilizable structural analogue, D-glucose, was found to either stimulate or inhibit beta-galactosidase formation depending upon its concentration. D-Arabinose, on the other hand, a non-utilizable structural analogue, is only capable of inhibiting, whereas succinic acid, a structurally unrelated energy source, is only capable of stimulating beta-galactosidase formation. 5. D-Arabinose inhibition of lactose-induced beta-galactosidase formation was found to be of the competitive type. 6. Some of the implications of these findings have been discussed.
...
PMID:The mechanism of the synthesis of enzymes. I. Development of a system suitable for studying this phenomenon. 1305 5

McClatchy, J. K. (The University of Texas, Dallas), and E. D. Rosenblum. Induction of lactose utilization in Staphylococcus aureus. J. Bacteriol. 86:1211-1215. 1963.-Adaptation to the utilization of lactose by Staphylococcus aureus has been compared with that by Escherichia coli. Lactose and galactose were found to be efficient inducers of the beta-galactosidase and the postulated galactoside-permease of S. aureus; the thiogalactosides, active as gratuitous inducers for E. coli, were inactive and inhibited induction of staphylococci by lactose and galactose. Mutants lacking beta-galactosidase or galactoside-permease, as well as a constitutive mutant for lactose utilization, were isolated. Like that in E. coli, the genetic system of staphylococcus seems to consist of two structural genes for the synthesis of the two enzymes and at least one regulatory gene simultaneously controlling the expression of the structural genes. The mutants were grouped by cross-transduction studies in three loci corresponding to the three phenotypes. Mutants of the pleiotropic locus were also isolated.
...
PMID:INDUCTION OF LACTOSE UTILIZATION IN STAPHYLOCOCCUS AUREUS. 1408 91

Citti, J. E. (Oregon State University, Corvallis), W. E. Sandine, and P. R. Elliker. beta-Galactosidase of Streptococcus lactis. J. Bacteriol. 89:937-942. 1965.-Synthesis of beta-galactosidase by several strains of Streptococcus lactis was induced by lactose. The rate of hydrolysis of o-nitrophenyl-beta-d-galactopyranoside was used to measure enzyme activity. The enzyme of all but one strain was unstable when whole cells were sonic-treated or treated with toluene; the enzyme of one strain of S. lactis was stable to these treatments, which resulted in at least a fivefold increase in activity over that found in whole cells. The optimal assay conditions for toluene-treated cells of this strain involved incubation at 37 C in pH 7.0 sodium phosphate buffer. Lactose was the most effective inducer of enzyme synthesis. Methyl-beta-d-thiogalactopyranoside, isopropyl-beta-d-thiogalactopyranoside, and galactose were also inducers of the enzyme, but were not as effective as lactose. Melibiose, maltose, and calcium lactobionate were poor inducers of enzyme synthesis. Exogenously supplied glucose repressed enzyme synthesis. The means of control of induced beta-galactosidase synthesis in S. lactis was similar to that in Escherichia coli.
...
PMID:BETA-GALACTOSIDASE OF STREPTOCOCCUS LACTIS. 1427 18

The cladoceran Daphnia pulex is well established as a model for ecotoxicology. Here, we show that D. pulex is also useful for investigating the effects of toxins on the heart in situ and the toxic effects in lactose intolerance. The mean heart rate at 10 degrees C was 195.9+/-27.0 beats/min (n=276, range 89.2-249.2, >80% 170-230 beats/min). D. pulex heart responded to caffeine, isoproteronol, adrenaline, propranolol and carbachol in the bathing medium. Lactose (50-200 mM) inhibited the heart rate by 30-100% (K(1/2)=60 mM) and generated severe arrhythmia within 60 min. These effects were fully reversible by 3-4 h. Sucrose (100-200 mM) also inhibited the heart rate, but glucose (100-200 mM) and galactose (100-200 mM) had no effect, suggesting that the inhibition by lactose or sucrose was not simply an osmotic effect. The potent antibiotic ampicillin did not prevent the lactose inhibition, and two diols known to be generated by bacteria under anaerobic conditions were also without effect. The lack of effect of l-ribose (2 mM), a potent inhibitor of beta-galactosidase, supported the hypothesis that lactose and other disaccharides may affect directly ion channels in the heart. The results show that D. pulex is a novel model system for studying effects of agonists and toxins on cell signalling and ion channels in situ.
...
PMID:Lactose causes heart arrhythmia in the water flea Daphnia pulex. 1546 69

Lactose is the only soluble and economically feasible carbon source for the production of cellulases or heterologous proteins regulated by cellulase expression signals by Hypocrea jecorina (Trichoderma reesei). We investigated the role of the major beta-galactosidase of H. jecorina in lactose metabolism and cellulase induction. A genomic copy of the bga1 gene was cloned, and this copy encodes a 1,023-amino-acid protein with a 20-amino-acid signal sequence. This protein has a molecular mass of 109.3 kDa, belongs to glycosyl hydrolase family 35, and is the major extracellular beta-galactosidase during growth on lactose. Its transcript was abundant during growth on l-arabinose and l-arabinitol but was much less common when the organism was grown on lactose, d-galactose, galactitol, d-xylose, and xylitol. Deltabga1 strains grow more slowly and accumulate less biomass on lactose, but the cellobiohydrolase I and II gene expression and the final cellulase yields were comparable to those of the parental strain. Overexpression of bga1 under the control of the pyruvate kinase promoter reduced the lag phase, increased growth on lactose, and limited transcription of cellobiohydrolases. We detected an additional extracellular beta-galactosidase activity that was not encoded by bga1 but no intracellular beta-galactosidase activity. In conclusion, cellulase production on lactose occurs when beta-galactosidase activity levels are low but decreases as the beta-galactosidase activities increase. The data indicate that bga1-encoded beta-galactosidase activity is a critical factor for cellulase production on lactose.
...
PMID:Role of the bga1-encoded extracellular {beta}-galactosidase of Hypocrea jecorina in cellulase induction by lactose. 1569 40

Goodman, R. E. (University of California, Los Angeles), and M. J. Pickett. Delayed lactose fermentation by Enterobacteriaceae. J. Bacteriol. 92:318-327. 1966.-When 171 Citrobacter freundii strains and 14 Paracolobactrum arizonae strains examined, 51 of the C. freundii strains and 13 of the P. arizonae strains were found to be delayed or negative lactose fermenters. Of the slow fermenters, 65% yielded rapidly fermenting mutants in cultures undergoing delayed fermentation. Lactose fermentation could generally be hastened by increasing lactose concentrations. Many organisms which fermented lactose slowly grew readily on a medium containing lactose as the sole carbon source. Regardless of their ability to ferment lactose, all strains of C. freundii and P. arizonae investigated could be shown to possess beta-galactosidase. Delayed fermenters failed to take up lactose from the culture medium, whereas prompt fermenters did so readily. The beta-galactosidases of 12 strains of enteric bacteria were studied in crude cell extracts with respect to specific activity, stability, and activity at varying substrate (o-nitrophenyl-beta-d-galactopyranoside) concentrations, at varying pH, and in the presence of sodium, potassium, and magnesium. The widely varying specific activities and the approximate similarity of the Michaelis constants (about 2 x 10(-4)m) suggested that the strains investigated produced differing amounts of beta-galactosidase. Moreover, qualitative differences in the enzymes provided evidence that these strains synthesized different molecular forms of beta-galactosidase. The results suggested that organisms which ferment lactose only after a prolonged delay do so because they possess multiple defects in their lactose-metabolizing machinery.
...
PMID:Delayed lactose fermentation by enterobacteriaceae. 1656 13

A cold-active beta-galactosidase of Antarctic marine bacterium Pseudoalteromonas sp. 22b was synthesized by an Escherichia coli transformant harboring its gene and immobilized on glutaraldehyde-treated chitosan beads. Unlike the soluble enzyme the immobilized preparation was not inhibited by glucose, its apparent optimum temperature for activity was 10 degrees C higher (50 vs. 40 degrees C, respectively), optimum pH range was wider (pH 6-9 and 6-8, respectively) and stability at 50 degrees C was increased whilst its pH-stability remained unchanged. Soluble and immobilized preparations of Antarctic beta-galactosidase were active and stable in a broad range of NaCl concentrations (up to 3 M) and affected neither by calcium ions nor by galactose. The activity of immobilized beta-galactosidase was maintained for at least 40 days of continuous lactose hydrolysis at 15 degrees C and its shelf life at 4 degrees C exceeded 12 months. Lactose content in milk was reduced by more than 90% over a temperature range of 4-30 degrees C in continuous and batch systems employing the immobilized enzyme.
...
PMID:Immobilized preparation of cold-adapted and halotolerant Antarctic beta-galactosidase as a highly stable catalyst in lactose hydrolysis. 1705 85

Galacto-oligosaccharides, complex mixtures of various sugars, are produced by transgalactosylation from lactose using beta-galactosidase and are of great interest for food and feed applications because of their prebiotic properties. Most galacto-oligosaccharide preparations currently available in the market contain a significant amount of monosaccharides and lactose. The mixture of galacto-oligosaccharides (GalOS) in this study produced from lactose using recombinant beta-galactosidase from Lactobacillus reuteri contains 48% monosaccharides, 26.5% lactose and 25.5% GalOS. To remove efficiently both monosaccharides and lactose from this GalOS mixture containing significant amounts of prebiotic non-lactose disaccharides, a biocatalytic approach coupled with subsequent chromatographic steps was used. Lactose was first oxidised to lactobionic acid using fungal cellobiose dehydrogenases, and then lactobionic acid and monosaccharides were removed by ion-exchange and size-exclusion chromatography. Two different cellobiose dehydrogenases (CDH), originating from Sclerotium rolfsii and Myriococcum thermophilum, were compared with respect to their applicability for this process. CDH from S. rolfsii showed higher specificity for the substrate lactose, and only few other components of the GalOS mixture were oxidised during prolonged incubation. Since these sugars were only converted once lactose oxidation was almost complete, careful control of the CDH-catalysed reaction will significantly reduce the undesired oxidation, and hence subsequent removal, of any GalOS components. Removal of ions and monosaccharides by the chromatographic steps gave an essentially pure GalOS product, containing less than 0.3% lactose and monosaccharides, in a yield of 60.3%.
...
PMID:Production of lactose-free galacto-oligosaccharide mixtures: comparison of two cellobiose dehydrogenases for the selective oxidation of lactose to lactobionic acid. 1835 95


<< Previous 1 2 3 4 5 6 7 Next >>

---