Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.
...
PMID:Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 0 44

The mouse mutants testicular feminization and sex reversal have been used to investigate hormone-mediated induction and repression of enzymes. Tfm/Y animals were already known to be androgen insensitive, rendering the androgen-inducible enzymes ADH and beta-glucuronidase noninducible because of an inherited deficiency of a cytosol androgen-receptor complex. The animals display female secondary sexual characteristics. Sxr/+,XX animals display male primary and secondary sexual characteristics with small testes. We demonstrate (1) that the Tfm mutation is pleiotropic, preventing repression of an androgen-repressible enzyme (ornithine aminotransferase) as well as induction of androgen-inducible enzymes, (2) that an estrogen-inducible enzyme (histidine decarboxylase) is not affected by the Tfm mutation, and (3) that Sxr/+,XX animals produce enough androgen for malelike activities of androgen-sensitive enzymes. It was also discovered that histidine decarboxylase repressed by androgen in normal animals, rather than being unaffected by it in Tfm/Y animals, is in fact induced. This unexpected phenomenon is discussed and an explanation is suggested for it.
...
PMID:Effect of the mouse mutants testicular feminization and sex reversal on hormone-mediated induction and repression of enzymes. 3 63

The liver cells of 8 rabbits fed for 12 to 16 weeks with a cholesterol diet showed a decrease of RNA and a stronger reactivity for acid phosphatase and beta-glucuronidase. The non-specific esterase showed a weaker reactivity in the cells with a larger amount of cholesterol and a stronger reaction in the cells with a smaller quantity of this substance. Several enzymes such as: diaphorases, those of the pentose shunt and respiratory cycle as well as those related to the metabolism of lipids, proteins and mucopolysaccharides showed a unconspicuous reactivity. The glycogen was found in a lesser amont in 6 out of 8 rabbits but with a higher concentration in 2 of them. The reactivity of UDPG-GT, active phosphorylase, F-1,6-PA, F-1,6-P Ald, LDH and ADH was stronger in the last 2 animals but weaker in the 6 others. In this 8 rabbit group the total phosphorylase and G-6-PA showed respectively always a stronger and a weaker reactivity than their controls. In the liver of 2 cholesterol-fed for 20 weeks rabbits it was observed a centrolobular fibrosis, a smaller amount of RNA and glycogen as well as a global decrease of the enzymatic reactivity.
...
PMID:Histochemical reactions of liver cells in cholesterol-fed rabbits. 40 25

Complementation of fission yeast mutants by plant genomic libraries could be a promising method for the isolation of novel plant genes. One important prerequisite is the functioning of plant promoters and terminators in Schizosaccharomyces pombe and Saccharomyces cerevisiae. Therefore, we studied the expression of the bacterial beta-glucuronidase (GUS) reporter gene under the control of the Cauliflower Mosaic Virus (CaMV) 35S promoter and 35S terminator. We show here that S. pombe initiates transcription at exactly the same start site as was reported for tobacco. The 35S CaMV terminator is appropriately recognized leading to a polyadenylated mRNA of the same size as obtained in plant cells transformed with the same construct. Furthermore, the GUS-mRNA is translated into fully functional GUS protein, as determined by an enzymatic assay. Interestingly, expression of the 35S promoter in the budding yeast S. cerevisiae was found to be only moderate and about hundredfold lower than in S. pombe. To investigate whether different transcript stabilities are responsible for this enormous expression difference in the two yeasts, the 35S promoter was substituted by the ADH (alcohol dehydrogenase) promoter from fission yeast. In contrast to the differential expression pattern of the 35S promoter, the ADH promoter resulted in equally high expression rates in both fission and budding yeast, comparable to the 35S promoter in S. pombe. Since the copy number of the 35S-GUS constructs differs only by a factor of two in the two yeasts, it appears that differential recognition of the 35S promoter is responsible for the different transcription rates.
...
PMID:Evolutionary conservation of transcriptional machinery between yeast and plants as shown by the efficient expression from the CaMV 35S promoter and 35S terminator. 220 23

The relationships between cAMP and hyaluronate hydrolases (HH) activity were studied in the renal tissue. Both the urine osmolality and the HH activity were increased in the papilla tissue of rats treated with cAMP. Incubation of mild homogenized cells prepared from kidney papilla with cAMP, resulted in a significant increase in the total HH activity and that of beta-glucuronidase and N-acetyl-beta-D-hexosaminidase, whereas the activity of hyaluronidase remained unchanged. The data obtained suggest that ADH effect on the HH activity is mediated by adenylate cyclase mechanism.
...
PMID:[Effect of cyclic 3',5'-adenosine monophosphate on hyaluronate hydrolase activity in the renal papilla]. 282 25

The gusA gene, encoding a new beta-glucuronidase enzyme, has been cloned from Lactobacillus gasseri ADH. This is the first report of a beta-glucuronidase gene cloned from a bacterial source other than Escherichia coli. A plasmid library of L. gasseri chromosomal DNA was screened for complementation of an E. coli gus mutant. Two overlapping clones that restored beta-glucuronidase activity in the mutant strain were sequenced and revealed three complete and two partial open reading frames. The largest open reading frame, spanning 1,797 bp, encodes a 597-amino-acid protein that shows 39% identity to beta-glucuronidase (GusA) of E. coli K-12 (EC 3.2.1.31). The other two complete open reading frames, which are arranged to be separately transcribed, encode a putative bile salt hydrolase and a putative protein of unknown function with similarities to MerR-type regulatory proteins. Overexpression of GusA was achieved in a beta-glucuronidase-negative L. gasseri strain by expressing the gusA gene, subcloned onto a low-copy-number shuttle vector, from the strong Lactobacillus P6 promoter. GusA was also expressed in E. coli from a pET expression system. Preliminary characterization of the GusA protein from crude cell extracts revealed that the enzyme was active across an acidic pH range and a broad temperature range. An analysis of other lactobacilli identified beta-glucuronidase activity and gusA homologs in other L. gasseri isolates but not in other Lactobacillus species tested.
...
PMID:Identification and cloning of gusA, encoding a new beta-glucuronidase from Lactobacillus gasseri ADH. 1122 18

An efficient method is described for the generation of site-specific chromosomal integrations in Lactobacillus acidophilus and Lactobacillus gasseri. The strategy is an adaptation of the lactococcal pORI system (K. Leenhouts, G. Venema, and J. Kok, Methods Cell Sci. 20:35-50, 1998) and relies on the simultaneous use of two plasmids. The functionality of the integration strategy was demonstated by the insertional inactivation of the Lactobacillus acidophilus NCFM lacL gene encoding beta-galactosidase and of the Lactobacillus gasseri ADH gusA gene encoding beta-glucuronidase.
...
PMID:Efficient system for directed integration into the Lactobacillus acidophilus and Lactobacillus gasseri chromosomes via homologous recombination. 1152 48

Whole-mount detection methods are quick, inexpensive and offer the possibility of studying the temporal and spatial patterns of gene expression in a morphological context. These methods have been used widely to detect messenger RNAs and to measure enzymatic activity of reporter genes, such as beta-galactosidase or beta-glucuronidase. Taking advantage of the fact that NADH generated during the oxidation of formaldehyde by class III alcohol dehydrogenase can reduce the compound nitroblue tetrazolium to form a blue precipitate, we have developed a new method to detect class III alcohol dehydrogenase activity in situ in whole Arabidopsis plants. This reaction has been used earlier for in situ electrophoresis detection and for histochemical analysis in animal tissue sections. With a few modifications, it can be used in whole Arabidopsis plants or excised plant tissues to allow a rapid analysis of class III ADH activity during development or in response to elicitors. The method might be extended to other dehydrogenases by using specific substrates.
...
PMID:Histochemical assay to detect class III ADH activity in situ in Arabidopsis seedlings. 1551 10

The Lactobacillus gasseri ADH beta-glucuronidase gene, gusA, was cloned previously and found to exhibit excellent activity in acidic pH ranges, with maximal activity at pH 5.0. In contrast, activity was limited in neutral pH ranges of 6-7. In an effort to improve the activity of the reporter enzyme in neutral pH ranges, the gusA gene was cloned into the broad host range vector, pGK12, and subjected to random mutagenesis by passage through Epicurian coli mutator strain XL1-Red. Two mutant alleles, gusA2 and gusA3, were recovered that produced beta-glucuronidase with increased activity in neutral pH ranges. One of these, gusA3, was significantly more active in the pH range of 4-8 in both Escherichia coli and L. gasseri. Sequence analysis of gusA2 and gusA3 revealed single base pair changes that resulted in D524G and D573A substitutions, respectively. The modified GusA3 enzyme has expanded potential for use as a reporter enzyme in expression hosts that are not acidophilic, as well as lactic acid bacteria and other microorganisms that grow in acidifying environments.
...
PMID:Modification of Lactobacillus beta-glucuronidase activity by random mutagenesis. 1717 82

The beta-glucuronidase (GUS) gene from Lactobacillus brevis RO1 was cloned and expressed in Escherichia coli GMS407. The GUS gene was composed of 1812 bp, encoding a 603-amino-acid protein belonging to the glycosyl hydrolase family 2 with three conserved domains. The amino acid similarity was higher than 70% with the beta-glucuronidases of various microorganisms, yet less than 58% with the beta-glucuronidase of L. gasseri ADH. Overexpression and purification of the GUS was performed in beta-glucuronidase-deficient E. coli GMS407. The purified GUS protein was 71 kDa and showed 1284 U/mg of specific activity at optimum condition of pH 5.0 and 37 degrees C. At 37 degrees C, the GUS remained stable for 80 min at pH values ranging from 5.0 to 8.0. The purified enzyme exhibited a half-life of 1 h at 60 degrees C and more than 2 h at 50 degrees C. When the purified GUS was applied to transform baicalin and wogonoside into their corresponding aglycones, 150 microM of baicalin and 125 microM of wogonoside were completely transformed into baicalein and wogonin, respectively, within 3 h.
...
PMID:Cloning and expression of beta-glucuronidase from Lactobacillus brevis in E. coli and application in the bioconversion of baicalin and wogonoside. 2007 33


1