Journal articles: 'Β-Glucuronidases'

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Bae, Hyung-Sup, Young-Suk Kim, Ki-Ho Cho, Kyung-Sup Lee, Jung-Jin Kim, Hae-Ung Lee, and Dong-Hyun Kim. "Hepatoprotective Activity of Reduohanxiao-tang (Yuldahanso-tang) is Related to the Inhibition of β-Glucuronidase." American Journal of Chinese Medicine 31, no. 01 (January 2003): 111–17. http://dx.doi.org/10.1142/s0192415x03000722.

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β-Glucuronidase-inhibitory and hepatoprotective effects of Reduohanxiao-tang (Yuldahanso-tang), which has been used for liver diseases and stroke, on carbon tetrachloride (CCl4)-induced hepatotoxicity of rats were investigated. Reduohanxiao-tang potently inhibited β-glucuronidases. Serum aspartate aminotransferase (AST), alanine aminotransferase (ALT) and lactic acid dehydrogenase (LDH) levels of the CCl4 group orally treated with Reduohanxiao-tang (100 mg/kg) were lowered to 54%, 71.5% and 66.1% of the CCl4-treated control group, respectively. Among the ingredients of the Reduohanxiao-tang, the rhizomes of Pueraria thunbergiana and it Scutellaria baicalensis potently inhibited β-glucuronidases and protected against CCl4-induced liver injury. Orally administered puerarin, which is a main component of Pueraria thunbergiana, showed potent hepatoprotective activity, but did not inhibit β-glucuronidase. However, daidzein, which is produced from puerarin by human intestinal bacteria, potently inhibited β-glucuronidase. These results suggest that β-glucuronidase inhibition by herbal medicines may protect a gainst CCl4-induced liver injury.

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Bai, Yue, Lu Chen, Yun-Feng Cao, Xu-Dong Hou, Shou-Ning Jia, Qi Zhou, Yu-Qi He, and Jie Hou. "Beta-Glucuronidase Inhibition by Constituents of Mulberry Bark." Planta Medica 87, no. 08 (March 17, 2021): 631–41. http://dx.doi.org/10.1055/a-1402-6431.

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AbstractIntestinal bacterial β-glucuronidases, the key enzymes responsible for the hydrolysis of various glucuronides into free aglycone, have been recognized as key targets for treating various intestinal diseases. This study aimed to investigate the inhibitory effects and mechanisms of the Mulberry bark constituents on E. coli β-glucuronidase (EcGUS), the most abundant β-glucuronidases produced by intestinal bacteria. The results showed that the flavonoids isolated from Mulberry bark could strongly inhibit E. coli β-glucuronidase, with IC50 values ranging from 1.12 µM to 10.63 µM, which were more potent than D-glucaric acid-1,4-lactone. Furthermore, the mode of inhibition of 5 flavonoids with strong E. coli β-glucuronidase inhibitory activity (IC50 ≤ 5 µM) was carefully investigated by a set of kinetic assays and in silico analyses. The results demonstrated that these flavonoids were noncompetitive inhibitors against E. coli β-glucuronidase-catalyzed 4-nitrophenyl β-D-glucuronide hydrolysis, with Ki values of 0.97 µM, 2.71 µM, 3.74 µM, 3.35 µM, and 4.03 µM for morin (1), sanggenon C (2), kuwanon G (3), sanggenol A (4), and kuwanon C (5), respectively. Additionally, molecular docking simulations showed that all identified flavonoid-type E. coli β-glucuronidase inhibitors could be well-docked into E. coli β-glucuronidase at nonsubstrate binding sites, which were highly consistent with these agentsʼ noncompetitive inhibition mode. Collectively, our findings demonstrated that the flavonoids in Mulberry bark displayed strong E. coli β-glucuronidase inhibition activity, suggesting that Mulberry bark might be a promising dietary supplement for ameliorating β-glucuronidase-mediated intestinal toxicity.

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Elmassry, Moamen M., Sunghwan Kim, and Ben Busby. "Predicting drug-metagenome interactions: Variation in the microbial β-glucuronidase level in the human gut metagenomes." PLOS ONE 16, no. 1 (January 7, 2021): e0244876. http://dx.doi.org/10.1371/journal.pone.0244876.

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Characterizing the gut microbiota in terms of their capacity to interfere with drug metabolism is necessary to achieve drug efficacy and safety. Although examples of drug-microbiome interactions are well-documented, little has been reported about a computational pipeline for systematically identifying and characterizing bacterial enzymes that process particular classes of drugs. The goal of our study is to develop a computational approach that compiles drugs whose metabolism may be influenced by a particular class of microbial enzymes and that quantifies the variability in the collective level of those enzymes among individuals. The present paper describes this approach, with microbial β-glucuronidases as an example, which break down drug-glucuronide conjugates and reactivate the drugs or their metabolites. We identified 100 medications that may be metabolized by β-glucuronidases from the gut microbiome. These medications included morphine, estrogen, ibuprofen, midazolam, and their structural analogues. The analysis of metagenomic data available through the Sequence Read Archive (SRA) showed that the level of β-glucuronidase in the gut metagenomes was higher in males than in females, which provides a potential explanation for the sex-based differences in efficacy and toxicity for several drugs, reported in previous studies. Our analysis also showed that infant gut metagenomes at birth and 12 months of age have higher levels of β-glucuronidase than the metagenomes of their mothers and the implication of this observed variability was discussed in the context of breastfeeding as well as infant hyperbilirubinemia. Overall, despite important limitations discussed in this paper, our analysis provided useful insights on the role of the human gut metagenome in the variability in drug response among individuals. Importantly, this approach exploits drug and metagenome data available in public databases as well as open-source cheminformatics and bioinformatics tools to predict drug-metagenome interactions.

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Yang, Wei, Bin Wei, and Ru Yan. "Amoxapine Demonstrates Incomplete Inhibition of β-Glucuronidase Activity from Human Gut Microbiota." SLAS DISCOVERY: Advancing the Science of Drug Discovery 23, no. 1 (August 15, 2017): 76–83. http://dx.doi.org/10.1177/2472555217725264.

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Amoxapine has been demonstrated to be a potent inhibitor of Escherichia coli β-glucuronidase. This study aims to explore the factors causing unsatisfactory efficacy of amoxapine in alleviating CPT-11–induced gastrointestinal toxicity in mice and to predict the outcomes in humans. Amoxapine (100 µM) exhibited poor and varied inhibition on β-glucuronidase activity in gut microbiota from 10 healthy individuals and their pool (pool, 11.9%; individuals, 3.6%−54.4%) with IC50 >100 µM and potent inhibition toward E. coli β-glucuronidase (IC50 = 0.34 µM). p-Nitrophenol formation from p-nitrophenyl-β-D-glucuronide by pooled and individual gut microbiota fitted classical Michaelis-Menten kinetics, showing similar affinity (Km = 113–189 µM) but varied catalytic capability (Vmax = 53–556 nmol/h/mg). Interestingly, amoxapine showed distinct inhibitory effects (8.7%–100%) toward β-glucuronidases of 13 bacterial isolates (including four Enterococcus, three Streptococcus, two Escherichia, and two Staphylococcus strains; gus genes belonging to OTU1, 2 or 21) regardless of their genetic similarity or bacterial origin. In addition, amoxapine inhibited the growth of pooled and individual gut microbiota at a high concentration (6.3%–30.8%, 200 µM). Taken together, these findings partly explain the unsatisfactory efficacy of amoxapine in alleviating CPT-11–induced toxicity and predict a poor outcome of β-glucuronidase inhibition in humans, highlighting the necessity of using a human gut microbiota community for drug screening.

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Wang, Xiaoyan, Yanli Liu, Chao Wang, Xudong Feng, and Chun Li. "Properties and structures of β-glucuronidases with different transformation types of glycyrrhizin." RSC Advances 5, no. 84 (2015): 68345–50. http://dx.doi.org/10.1039/c5ra11484e.

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6

Correa, Sonali, Magdalena Ripoll, Erienne Jackson, Valeria Grazú, and Lorena Betancor. "Stabilization of b-Glucuronidase by Immobilization in Magnetic-Silica Hybrid Supports." Catalysts 10, no. 6 (June 13, 2020): 669. http://dx.doi.org/10.3390/catal10060669.

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β-Glucuronidases are a class of enzymes that catalyze the breakdown of complex carbohydrates. They have well documented biocatalytic applications in synthesis, therapeutics, and analytics that could benefit from enzyme immobilization and stabilization. In this work, we have explored a number of immobilization strategies for Patella vulgata β-Glucuronidase that comprised a tailored combination of biomimetic silica (Si) and magnetic nanoparticles (MNPs). The individual effect of each material on the enzyme upon immobilization was first tested. Three different immobilization strategies for covalent attachment on MNPs and different three catalysts for the deposition of Si particles were tested. We produced nine different immobilized preparations and only two of them presented negligible activity. All the preparations were in the micro-sized range (from 1299 ± 52 nm to 2101 ± 67 nm of hydrodynamic diameter). Their values for polydispersity index varied around 0.3, indicating homogeneous populations of particles with low probability of agglomeration. Storage, thermal, and operational stability were superior for the enzyme immobilized in the composite material. At 80 °C different preparations with Si and MNPs retained 40% of their initial activity after 6 h of incubation whereas the soluble enzyme lost 90% of its initial activity within 11 min. Integration of MNPs provided the advantage of reusing the biocatalyst via magnetic separation up to six times with residual activity. The hybrid material produced herein demonstrated its versatility and robustness as a support for β-Glucuronidases immobilization.

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Wong, Alexander W., Shouming He, and Stephen G. Withers. "Synthesis of 5-fluoro-β-D-glucopyranosyluronic acid fluoride and its evaluation as a mechanistic probe of Escherichia coli β-glucuronidase." Canadian Journal of Chemistry 79, no. 5-6 (May 1, 2001): 510–18. http://dx.doi.org/10.1139/v00-155.

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Synthesis of the potential mechanism-based inactivator of β-D-glucuronidases (5-fluoro-β-D-glucopyranosyluronic acid fluoride) was accomplished via a six-step process from D-glucuronic acid that involved radical bromination at C-5 and displacement of the bromide by fluoride. A key step in this process was the masking of the carboxylic acid as a phenacyl ester. This group is uniquely stable to conditions of photobromination and fluoride displacement, yet removable under very mild conditions. Incubation of the Escherichia coli β-glucuronidase with 5-fluoro-β-D-glucopyranosyluronic acid fluoride resulted in time-dependent inactivation of the enzyme through the accumulation of a covalent 5-fluoro-α-D-glucopyranosyluronic acid-enzyme. Peptic digestion of the 5-fluoro-α-D-glucopyranosyluronic acid-enzyme intermediate and subsequent analysis by liquid chromatography coupled to an electrospray ionization triple quadrupole mass spectrometer indicated the presence of a 5-fluoro-α-D-glucopyranosyluronic acid-modified peptide. This peptide was partially purified by HPLC and its sequence determined by tandem mass spectrometry in the daughter ion scan mode, permitting the identification of Glu504 as the catalytic nucleophile within the sequence ITEYGVD. This new reagent is therefore useful for the specific, mechanism-based inactivation of glycuronidases and has good potential in other studies of enzymes of this general class.Key words: β-glucuronidase, catalytic nucleophile, 5-fluoro-β-D-glucopyranosyluronic acid fluoride, electrospray MS.

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8

Wu, Liang, Jianbing Jiang, Yi Jin, Wouter W. Kallemeijn, Chi-Lin Kuo, Marta Artola, Wei Dai, et al. "Activity-based probes for functional interrogation of retaining β-glucuronidases." Nature Chemical Biology 13, no. 8 (June 5, 2017): 867–73. http://dx.doi.org/10.1038/nchembio.2395.

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9

Pollet, Rebecca M., Emma H. D'Agostino, William G. Walton, Yongmei Xu, Michael S. Little, Kristen A. Biernat, Samuel J. Pellock, et al. "An Atlas of β-Glucuronidases in the Human Intestinal Microbiome." Structure 25, no. 7 (July 2017): 967–77. http://dx.doi.org/10.1016/j.str.2017.05.003.

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10

Canales, I., A. Manjōn, and J. L. Iborra. "Immobilization of β-glucuronidases on an epoxy-activated polyacrylic matrix." Biotechnology Techniques 4, no. 3 (May 1990): 205–10. http://dx.doi.org/10.1007/bf00222507.

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11

Ervin, Samantha M., Ronan P. Hanley, Lauren Lim, William G. Walton, Kenneth H. Pearce, Aadra P. Bhatt, Lindsey I. James, and Matthew R. Redinbo. "Targeting Regorafenib-Induced Toxicity through Inhibition of Gut Microbial β-Glucuronidases." ACS Chemical Biology 14, no. 12 (October 30, 2019): 2737–44. http://dx.doi.org/10.1021/acschembio.9b00663.

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12

Teplitsky, Anna, Smadar Shulami, Sara Moryles, Galia Zaide, Yuval Shoham, and Gil Shoham. "Crystallization and preliminary X-ray analysis of α-D-glucuronidase from Bacillus stearothermophilus T-6." Acta Crystallographica Section D Biological Crystallography 55, no. 4 (April 1, 1999): 869–72. http://dx.doi.org/10.1107/s0907444998012918.

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α-D-Glucuronidases cleave the α-1,2-glycosidic bond of the 4-O-methyl-α-D-glucuronic acid side chain in xylan. Of the xylan-debranching hydrolases, these enzymes are the least studied and characterized. The α-glucuronidase gene (aguA) from Bacillus stearothermophilus T-6 has been cloned, sequenced and overproduced in Escherichia coli. The gene encodes for a protein of 679 amino acids with a calculated molecular weight of 78480 and a pI of 5.42. α-Glucuronidase T-6 shows high homology to the α-glucuronidases of Thermotoga maritima (60% identity) and of Trichoderma reesei (44% identity). Based on the amino-acid sequence similarity, it is likely that these enzymes represent a new class of glycosyl hydrolases. Crystallographic studies of α-glucuronidase T-6 were initiated to study the mechanism of catalysis, as well as to provide a structural basis for rational introduction of enhanced thermostability by site-specific mutagenesis. In this report, the crystallization and preliminary crystallographic characterization of the native α-glucuronidase T-6 enzyme is described. Two crystal forms were found suitable for detailed crystal structure analysis. The T1 form was obtained by the vapour-diffusion method using PEG 4000 as a precipitant and 2-propanol as an organic additive. The crystals belong to a primitive tetragonal crystal system (space group P41212 or P43212) with unit-cell dimensions a = b = 76.1 and c = 331.2 Å. These crystals are mechanically strong, are stable in the X-ray beam and diffract X-rays to better than 2.4 Å resolution. A full 3.0 Å resolution diffraction data set (97.3% completeness, R merge 9.8%) has recently been collected on one crystal at room temperature using a rotating-anode X-ray source and an R-AXIS IIc imaging-plate detector. The M1 form was obtained and characterized by similar techniques. The best crystallization occurred at a slightly lower pH and a lower concentration of 2-propanol. The crystals belong to a primitive monoclinic crystal system (space group P21) with unit-cell dimensions a = 65.8, b = 127.4, c = 96.6 Å and β = 97.9°. These crystals are also quite strong and stable, and diffract to better than 2.8 Å resolution. A full 2.8 Å resolution diffraction data set (96.2% completeness, R merge 7.6%) has recently been collected on one crystal at room temperature using the same R-AXIS IIc setup. Both forms are currently being used to obtain crystallographic phasing via isomorphous heavy-atom derivatives and selenomethionine MAD experiments.

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Liu, Mingzhu, Jing Yu, Bo Lv, Yuhui Hou, Xinhe Liu, Xudong Feng, and Chun Li. "Improving the activity and thermostability of GH2 β‐glucuronidases via domain reassembly." Biotechnology and Bioengineering 118, no. 5 (February 19, 2021): 1962–72. http://dx.doi.org/10.1002/bit.27710.

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14

Konishi, Tomoyuki, Toshihisa Kotake, Dina Soraya, Koji Matsuoka, Tetsuo Koyama, Satoshi Kaneko, Kiyohiko Igarashi, Masahiro Samejima, and Yoichi Tsumuraya. "Properties of family 79 β-glucuronidases that hydrolyze β-glucuronosyl and 4-O-methyl-β-glucuronosyl residues of arabinogalactan-protein." Carbohydrate Research 343, no. 7 (May 2008): 1191–201. http://dx.doi.org/10.1016/j.carres.2008.03.004.

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Pellock, Samuel J., William G. Walton, Kristen A. Biernat, Dariana Torres-Rivera, Benjamin C. Creekmore, Yongmei Xu, Jian Liu, Ashutosh Tripathy, Lance J. Stewart, and Matthew R. Redinbo. "Three structurally and functionally distinct β-glucuronidases from the human gut microbeBacteroides uniformis." Journal of Biological Chemistry 293, no. 48 (October 9, 2018): 18559–73. http://dx.doi.org/10.1074/jbc.ra118.005414.

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Pellock, Samuel J., William G. Walton, Samantha M. Ervin, Dariana Torres-Rivera, Benjamin C. Creekmore, Grace Bergan, Zachary D. Dunn, Bo Li, Ashutosh Tripathy, and Matthew R. Redinbo. "Discovery and Characterization of FMN-Binding β-Glucuronidases in the Human Gut Microbiome." Journal of Molecular Biology 431, no. 5 (March 2019): 970–80. http://dx.doi.org/10.1016/j.jmb.2019.01.013.

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Schlachter, Caleb R., Amanda C. McGee, Pongkwan N. Sitasuwan, Gary C. Horvath, Nanda G. Karri, L. Andrew Lee, and John J. Tomashek. "Variants of glycosyl hydrolase family 2 β-glucuronidases have increased activity on recalcitrant substrates." Enzyme and Microbial Technology 145 (April 2021): 109742. http://dx.doi.org/10.1016/j.enzmictec.2020.109742.

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Ervin, Samantha M., Hao Li, Lauren Lim, Lee R. Roberts, Xue Liang, Sridhar Mani, and Matthew R. Redinbo. "Gut microbial β-glucuronidases reactivate estrogens as components of the estrobolome that reactivate estrogens." Journal of Biological Chemistry 294, no. 49 (October 21, 2019): 18586–99. http://dx.doi.org/10.1074/jbc.ra119.010950.

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Malgas, Samkelo, Mpho S. Mafa, Brian N. Mathibe, and Brett I. Pletschke. "Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation." Molecules 26, no. 22 (November 9, 2021): 6770. http://dx.doi.org/10.3390/molecules26226770.

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Enzymes classified with the same Enzyme Commission (EC) that are allotted in different glycoside hydrolase (GH) families can display different mechanisms of action and substrate specificities. Therefore, the combination of different enzyme classes may not yield synergism during biomass hydrolysis, as the GH family allocation of the enzymes influences their behavior. As a result, it is important to understand which GH family combinations are compatible to gain knowledge on how to efficiently depolymerize biomass into fermentable sugars. We evaluated GH10 (Xyn10D and XT6) and GH11 (XynA and Xyn2A) β-xylanase performance alone and in combination with various GH family α-l-arabinofuranosidases (GH43 AXH-d and GH51 Abf51A) and α-d-glucuronidases (GH4 Agu4B and GH67 AguA) during xylan depolymerization. No synergistic enhancement in reducing sugar, xylose and glucuronic acid released from beechwood xylan was observed when xylanases were supplemented with either one of the glucuronidases, except between Xyn2A and AguA (1.1-fold reducing sugar increase). However, overall sugar release was significantly improved (≥1.1-fold reducing sugar increase) when xylanases were supplemented with either one of the arabinofuranosidases during wheat arabinoxylan degradation. Synergism appeared to result from the xylanases liberating xylo-oligomers, which are the preferred substrates of the terminal arabinofuranosyl-substituent debranching enzyme, Abf51A, allowing the exolytic β-xylosidase, SXA, to have access to the generated unbranched xylo-oligomers. Here, it was shown that arabinofuranosidases are key enzymes in the efficient saccharification of hetero-xylan into xylose. This study demonstrated that consideration of GH family affiliations of the carbohydrate-active enzymes (CAZymes) used to formulate synergistic enzyme cocktails is crucial for achieving efficient biomass saccharification.

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Wallace, Bret D., Adam B. Roberts, Rebecca M. Pollet, James D. Ingle, Kristen A. Biernat, Samuel J. Pellock, Madhu Kumar Venkatesh, et al. "Structure and Inhibition of Microbiome β-Glucuronidases Essential to the Alleviation of Cancer Drug Toxicity." Chemistry & Biology 22, no. 9 (September 2015): 1238–49. http://dx.doi.org/10.1016/j.chembiol.2015.08.005.

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21

Nishimura, Yukio, Keitaro Kato, and Masaru Himeno. "Biochemical Characterization of Liver Microsomal, Golgi, Lysosomal, and Serum β-Glucuronidases in Dibuty1 Phosphate-Treated Rats1." Journal of Biochemistry 118, no. 1 (July 1995): 56–66. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a124892.

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22

Ebuzoeme, Christabel, Imoh Etim, Autumn Ikimi, Jamie Song, Ting Du, Ming Hu, Dong Liang, and Song Gao. "Glucuronides Hydrolysis by Intestinal Microbial β-Glucuronidases (GUS) Is Affected by Sampling, Enzyme Preparation, Buffer pH, and Species." Pharmaceutics 13, no. 7 (July 8, 2021): 1043. http://dx.doi.org/10.3390/pharmaceutics13071043.

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Glucuronides hydrolysis by intestinal microbial β-Glucuronidases (GUS) is an important procedure for many endogenous and exogenous compounds. The purpose of this study is to determine the impact of experimental conditions on glucuronide hydrolysis by intestinal microbial GUS. Standard probe 4-Nitrophenyl β-D-glucopyranoside (pNPG) and a natural glucuronide wogonoside were used as the model compounds. Feces collection time, buffer conditions, interindividual, and species variations were evaluated by incubating the substrates with enzymes. The relative reaction activity of pNPG, reaction rates, and reaction kinetics for wogonoside were calculated. Fresh feces showed the highest hydrolysis activities. Sonication increased total protein yield during enzyme preparation. The pH of the reaction system increased the activity in 0.69–1.32-fold, 2.9–12.9-fold, and 0.28–1.56-fold for mouse, rat, and human at three different concentrations of wogonoside, respectively. The Vmax for wogonoside hydrolysis was 2.37 ± 0.06, 4.48 ± 0.11, and 5.17 ± 0.16 μmol/min/mg and Km was 6.51 ± 0.71, 3.04 ± 0.34, and 0.34 ± 0.047 μM for mouse, rat, and human, respectively. The inter-individual difference was significant (4–6-fold) using inbred rats as the model animal. Fresh feces should be used to avoid activity loss and sonication should be utilized in enzyme preparation to increase hydrolysis activity. The buffer pH should be appropriate according to the species. Inter-individual and species variations were significant.

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Miyazaki, Kohji, Hiroyuki Miyamoto, Derry K. Mercer, Tatsuaki Hirase, Jennifer C. Martin, Yoichi Kojima, and Harry J. Flint. "Involvement of the Multidomain Regulatory Protein XynR in Positive Control of Xylanase Gene Expression in the Ruminal Anaerobe Prevotella bryantii B14." Journal of Bacteriology 185, no. 7 (April 1, 2003): 2219–26. http://dx.doi.org/10.1128/jb.185.7.2219-2226.2003.

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ABSTRACT The xylanase gene cluster from the rumen anaerobe Prevotella bryantii B14 was found to include a gene (xynR) that encodes a multidomain regulatory protein and is downstream from the xylanase and β-xylosidase genes xynA and xynB. Additional genes identified upstream of xynA and xynB include xynD, which encodes an integral membrane protein that has homology with Na:solute symporters; xynE, which is related to the genes encoding acylhydrolases and arylesterases; and xynF, which has homology with the genes encoding α-glucuronidases. XynR includes, in a single 833-amino-acid polypeptide, a putative input domain unrelated to other database sequences, a likely transmembrane domain, histidine kinase motifs, response regulator sequences, and a C-terminal AraC-type helix-turn-helix DNA binding domain. Two transcripts (3.7 and 5.8 kb) were detected with a xynA probe, and the start site of the 3.7-kb transcript encoding xynABD was mapped to a position upstream of xynD. The DNA binding domain of XynR was purified after amplification and overexpression in Escherichia coli and was found to bind to a 141-bp DNA fragment from the region immediately upstream of xynD. In vitro transcription assays demonstrated that XynR stimulates transcription of the 3.7-kb transcript. We concluded that XynR acts as a positive regulator that activates expression of xynABD in P. bryantii B14. This is the first regulatory protein that demonstrates significant homology with the two-component regulatory protein superfamily and has been shown to be involved in the regulation of polysaccharidase gene expression.

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Sitasuwan, Pongkwan, Cathleen Melendez, Margarita Marinova, Michelle Spruill, and L. Andrew Lee. "Comparison of Purified β-glucuronidases in Patient Urine Samples Indicates a Lack of Correlation Between Enzyme Activity and Drugs of Abuse Metabolite Hydrolysis Efficiencies Leading to Potential False Negatives." Journal of Analytical Toxicology 43, no. 3 (December 5, 2018): 221–27. http://dx.doi.org/10.1093/jat/bky082.

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25

Lee, Jo Ellen Sheets. "β-Glucuronidase Deficiency." American Journal of Diseases of Children 139, no. 1 (January 1, 1985): 57. http://dx.doi.org/10.1001/archpedi.1985.02140030059029.

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Sacco, C., and E. J. Calabrese. "Selective Inhibition of Gastrointestinal β-Glucuronidase by Poly(vinylbenzyl D-glucaro(1,4)lactonate). Part 2. Poly(vinylbenzyl D-Glucaro(1,4) lactonate) In vitro Inhibition Studies." Human & Experimental Toxicology 13, no. 11 (November 1994): 759–63. http://dx.doi.org/10.1177/096032719401301104.

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In vitro inhibition studies with β-glucuronidase from purified E. coli and mouse intestinal contents indicated that the polymer, poly(vinylbenzyl D-glucaro(1,4)lactonate, is an effective β-glucuronidase inhibitor. Purified E. coli β-glucuronidase was inhibited by 99.6% with 1 77 mM D-glucaro(1,4)lactone using the polymer-inhibitor. Similarly, 95% inhibition of β-glucuronidase activity of mouse intestinal contents was obtained with 177 mM and 50% inhibition was obtained with 31.5 mM D-glucaro(1,4)lactone based on the modified polymer. The structural requirements of an effective β-glucuronidase inhibitor based on the structure of the polymer-inhibitor are also discussed.

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Besse, Helena C., Yinan Chen, Hans W. Scheeren, Josbert M. Metselaar, Twan Lammers, Chrit T. W. Moonen, Wim E. Hennink, and Roel Deckers. "A Doxorubicin-Glucuronide Prodrug Released from Nanogels Activated by High-Intensity Focused Ultrasound Liberated β-Glucuronidase." Pharmaceutics 12, no. 6 (June 10, 2020): 536. http://dx.doi.org/10.3390/pharmaceutics12060536.

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The poor pharmacokinetics and selectivity of low-molecular-weight anticancer drugs contribute to the relatively low effectiveness of chemotherapy treatments. To improve the pharmacokinetics and selectivity of these treatments, the combination of a doxorubicin-glucuronide prodrug (DOX-propGA3) nanogel formulation and the liberation of endogenous β-glucuronidase from cells exposed to high-intensity focused ultrasound (HIFU) were investigated in vitro. First, a DOX-propGA3-polymer was synthesized. Subsequently, DOX-propGA3-nanogels were formed from this polymer dissolved in water using inverse mini-emulsion photopolymerization. In the presence of bovine β-glucuronidase, the DOX-propGA3 in the nanogels was quantitatively converted into the chemotherapeutic drug doxorubicin. Exposure of cells to HIFU efficiently induced liberation of endogenous β-glucuronidase, which in turn converted the prodrug released from the DOX-propGA3-nanogels into doxorubicin. β-glucuronidase liberated from cells exposed to HIFU increased the cytotoxicity of DOX-propGA3-nanogels to a similar extend as bovine β-glucuronidase, whereas in the absence of either bovine β-glucuronidase or β-glucuronidase liberated from cells exposed to HIFU, the DOX-propGA3-nanogels hardly showed cytotoxicity. Overall, DOX-propGA3-nanogels systems might help to further improve the outcome of HIFU-related anticancer therapy.

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Hijová, Emília, Jozef Kuzma, Ladislav Strojný, Alojz Bomba, Izabela Bertková, Anna Chmelárová, Zdena Hertelyová, Lucia Kuliková, Jana Štofilová, and Ľuboš Ambro. "Effect of Lactobacillus plantarum LS/07 on Intestinal Bacterial Enzyme Activities in the Prevention of Cancer, Atherosclerosis and Dysbiosis." Acta Veterinaria 66, no. 3 (September 1, 2016): 294–303. http://dx.doi.org/10.1515/acve-2016-0026.

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Abstract The effect of the probiotic strain Lactobacillus plantarum LS/07 on intestinal bacterial enzyme activities – β-glucuronidase (β-GLUCUR), β-galactosidase (β-GAL), and β-glucosidase (β-GLU) in the prevention of cancer, atherosclerosis and dysbiosis was investigated. Male Sprague-Dawley rats were randomly divided into 12 experimental groups: C (control group), AT (atherosclerotic group), CC (carcinogenic group), and then each group in combination with antibiotics and probiotics individually and each group in double combination on antibiotic and probiotic. In the control group the β-glucuronidase activity did not change throughout the experiment. High fat diet in the atherosclerotic group significantly increased the activity of β-glucuronidase (p<0.001) and β-glucosidase (p<0.01). Azoxymethane application in the carcinogenic group significantly increased β-glucuronidase (p<0.01), but reduced β-glucosidase (p<0.01). Daily application of probiotics individually and in double combination with antibiotics increased the activity of β-galactosidase, and β-glucosidase, and positively decreased the level of β-glucuronidase. In the control antibiotic group β-glucuronidase was significantly increased (p<0.05), and β-glucosidase decreased (p<0.01) which can be caused by a change of microflora in favor of coliform bacteria. These finding indicate the positive effects of probiotic Lactobacillus plantarum LS/07 which allows its use in disease prevention in human and veterinary medicine.

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Duchesne, Luc C., and Pierre J. Charest. "Effect of promoter sequence on transient expression of the β-glucuronidase gene in embryogenic calli of Larix × eurolepis and Picea mariana following microprojection." Canadian Journal of Botany 70, no. 1 (January 1, 1992): 175–80. http://dx.doi.org/10.1139/b92-023.

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The transient expression of the β-glucuronidase reporter gene was compared in embryogenic cell lines of Larix × eurolepis (L. decidua × L. leptolepis) and Picea mariana after introduction of eight vectors containing different promoter sequences using the Dupont Biolistic™ particle delivery system. Transient β-glucuronidase gene expression was highest in cells of both species after bombardment using the wheat abscisic acid inducible Em gene promoter. Transient β-glucuronidase gene expression was comparable in P. mariana and L. × eurolepis for all vectors, with the exception of the rice actin promoter that yielded higher activity in P. mariana than in L. × eurolepis. The Em gene promoter proved inducible by abscisic acid; upon the addition of abscisic acid to the culture medium, β-glucuronidase gene expression was increased 2.3- and 4.4-fold for L. × eurolepis and P. mariana, respectively. Investigation of β-glucuronidase gene expression over time showed that all transient activity disappeared 16 days after microprojection. Key words: Larix, Picea, transformation, β-glucuronidase, tissue cultures.

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Anouar, El Hassane, Moustapha Eid Moustapha, Muhammad Taha, Mohammed H. Geesi, Zeinab R. Farag, Fazal Rahim, Noor Barak Almandil, Rai Khalid Farooq, Muhammad Nawaz, and Ashik Mosaddik. "Synthesis, Molecular Docking and β-Glucuronidase Inhibitory Potential of Indole Base Oxadiazole Derivatives." Molecules 24, no. 5 (March 8, 2019): 963. http://dx.doi.org/10.3390/molecules24050963.

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β-glucuronidase is a lysosomal glycosidase enzyme which catalyzes the extracellular matrix of cancer and normal cells and the glycosaminoglycans of the cell membrane, which is important for cancer cell proliferation, invasion, and metastasis. Liver cancer, colon carcinoma, and neoplasm bladder are triggered by the increase of the level of β-glucuronidase activity. The most valuable structures are indole and oxadiazole which has gain immense attention because of its pharmacological behavior and display many biological properties. Twenty-two (1–22) analogs of indole based oxadiazole were synthesized and screened for their inhibitory potential against β-glucuronidase. Majority of the compounds showed potent inhibitory potential with IC50 values ranging between 0.9 ± 0.01 to 46.4 ± 0.9 µM, under positive control of standard drug d-saccharic acid 1,4 lactone (IC50 = 48.1 ± 1.2 µM). Structural activity relationship (SAR) has been established for all synthesized compounds. To shed light on molecular interactions between the synthesized compounds and β-glucuronidase, 1, 4, and 6 compounds were docked into the active binding site of β-glucuronidase. The obtained results showed that this binding is thermodynamically favorable and β-glucuronidase inhibition of the selected compounds increases with the number of hydrogen bonding established in selected compound-β-glucuronidase complexes.

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Sabbe, MB, D. Desruelles, and W. Lissens. "Is β-glucuronidase a clinical useful biomarker for an acute organophosphorus poisoning?" Human & Experimental Toxicology 27, no. 5 (May 2008): 431–33. http://dx.doi.org/10.1177/0960327108094614.

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β-glucuronidase is considered a sensitive biomarker for acute organophosphorus poisoning. In this well-documented study, multiple plasma samples over time were collected. A decrease in plasma concentration of β-glucuronidase was surprisingly observed, even within normal range. These findings do not support the hypothesis that β-glucuronidase is a useful biomarker for acute organophosphorus poisoning in humans.

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Lindop, Rosemary, Clifford Tasman-Jones, Lindy L. Thomsen, and Sum P. Lee. "Cellulose and pectin alter intestinal β-glucuronidase (EC 3.2.1.31) in the rat." British Journal of Nutrition 54, no. 1 (July 1985): 21–26. http://dx.doi.org/10.1079/bjn19850088.

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1. Groups of rats were given a fibre-free diet containing none or one of the three fibre components: pectin, cellulose or galactomannan.2. After feeding for 16 weeks, total protein level and β-glucuronidase (EC 3.2.1.31) activity in the contents and mucosa of jejunum and ileum, and in the contents only of the caecum, were determined.3. The pectin supplement reduced protein concentration in jejunal contents while cellulose reduced protein concentration in the ileal and caecal contents.4. β-Glucuronidase activity of caecal contents was significantly reduced in both the pectin- and cellulose-fed groups.5. Cellulose affected the β-glucuronidase activity of both the ileal contents while pectin reduced the β-glucuronidase of the ileal but not the jejunal contents.6. Dietary fibre components did not significantly affect jejunal or ileal mucosal β-glucuronidase activity.

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Stein, Colleen S., Abdi Ghodsi, Todd Derksen, and Beverly L. Davidson. "Systemic and Central Nervous System Correction of Lysosomal Storage in Mucopolysaccharidosis Type VII Mice." Journal of Virology 73, no. 4 (April 1, 1999): 3424–29. http://dx.doi.org/10.1128/jvi.73.4.3424-3429.1999.

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ABSTRACT Mucopolysaccharidosis (MPS) type VII patients lack functional β-glucuronidase, leading to systemic and central nervous system dysfunction. In this study we tested whether recombinant adenovirus that encodes β-glucuronidase (Adβgluc), delivered intravenously and into the brain parenchyma of MPS type VII mice, could provide long-term transgene expression and correction of lysosomal distension. We also tested whether systemic treatment with the immunosuppressive anti-CD40 ligand antibody, MR-1, affected transgene expression. We found substantial plasma β-glucuronidase activity for over 9 weeks after gene transfer in the MR-1- treated group, with subsequent decline in activity corresponding to a delayed anti-β-glucuronidase antibody response. At 16 weeks, near wild-type amounts of β-glucuronidase activity and striking reduction of lysosomal pathology were detected in livers from mice that had received either MR-1 cotreatment or control antibody. In the lung and kidney, β-glucuronidase activity was markedly higher for the MR-1-treated group. β-Glucuronidase activity in the brain persisted independently of MR-1 treatment. Activity was intense in the injected hemisphere and was also evident in the noninjected cortex and striatum, with dramatic improvements in storage deposits in areas of both hemispheres. These results indicate that prolonged enzyme expression from transgenes delivered to deficient liver and brain can mediate pervasive correction and illustrate the potential for gene therapy of MPS and other lysosomal storage diseases.

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Larsen, Torben, and Karen Aulrich. "Optimizing the fluorometric β-glucuronidase assay in ruminant milk for a more precise determination of mastitis." Journal of Dairy Research 79, no. 1 (September 23, 2011): 7–15. http://dx.doi.org/10.1017/s0022029911000720.

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Activity of the enzyme β-glucuronidase (EC 3.2.1.31) is found in milk from ruminants with mastitis. However, the use of this enzymic activity as an indicator of mastitis has gained little attention possibly because of its low activity when compared with other mastitis indicators. The determination may therefore be less precise and the analytical procedure very time consuming and labour intensive. The present study optimized the fluorometric determination of the β-glucuronidase activity with respect to substrate concentration, pH, incubation time etc., validated the assay, and developed it into large scale analyses. The assay performance is satisfactory regarding precision, linearity etc., and it appears comparable to analogous fluorometric assays for mastitis indicators in milk. From a local dairy herd, 825 milk samples were analysed for potential mastitis indicators, i.e. β-glucuronidase, lactate dehydrogenase (LDH), alkaline phosphatase (AP), and N-acetyl-β-d-glucosaminidase (NAGase) activity, and for somatic cell counts (SCC) and the variables were compared. Activity of β-glucuronidase was moderately but significantly correlated to SCC (r=0·21;n=768) as well as the other mentioned variables (r=0·25–0·43;n=825). Simple indices based on β-glucuronidase and LDH or NAGase activity were tested as indicators of mastitis (SCC), but were not found to improve the diagnostic value. Future studies may further verify whether β-glucuronidase can compete with well-established indicators of mastitis in cows such as LDH or NAGase as well as determine whether β-glucuronidase activity, in combination with other indicators of mastitis, has an advantage. Nineteen milk samples from subclinical and latent cases of mastitis (individual quarters) were identified for specific pathogens (PCR method) and measured for β-glucuronidase activity. The activity was tested at four different pH levels (5·5, 6·0, 6·5 and 7·0) in order to investigate the possibility of discrimination between pathogens. However, all milk samples (strains of pathogens) had the same pH optimum for β-glucuronidase activity; this may indicate that enzymic activity from mammary tissue and leucocytes dominates over enzyme activity from bacterial cells.

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ROY, DENIS, and PIERRE WARD. "Rapid Detection of Bifidobacterium dentium by Enzymatic Hydrolysis of β-Glucuronide Substrates." Journal of Food Protection 55, no. 4 (April 1, 1992): 291–95. http://dx.doi.org/10.4315/0362-028x-55.4.291.

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Enzyme profiles and fermentation patterns of bifidobacteria were studied to determine phenotypic characteristics that allow the rapid detection of Bifidobacterium dentium and its differentiation from Bifidobacterium adolescentis, Bifidobacterium angulatum, Bifidobacterium catenulatum, and Bifidobacterium pseudocatenulatum. Among 43 bifidobacterial strains tested, the production of β-glucuronidase was limited to six strains of B. dentium. The presence of B. dentium on a selective medium may be rapidly confirmed by the detection of β-glucuronidase activity. Columbia agar containing propionic acid was chosen to enumerate bifidobacteria previously cultivated in MRS medium. After 48 h of incubation, β-glucuronidase activity was determined by using a plate staining procedure. B. dentium strains gave positive results for β-glucuronidase activity after application of the overlay solution of β-glucuronide substrate. The β-glucuronidase assay is a rapid screening method for B. dentium. This method might be useful for selection of nonpathogenic strains or detection of fecal contamination from human origin.

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Shadix, Lois C., and Eugene W. Rice. "Evaluation of β-glucuronidase assay for the detection of Escherichia coli from environmental waters." Canadian Journal of Microbiology 37, no. 12 (December 1, 1991): 908–11. http://dx.doi.org/10.1139/m91-157.

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The new United States Drinking Water Regulations state that water systems must analyze for Escherichia coli or fecal coliforms on any routine or repeat sample that is positive for total coliforms. The proposed methods for the detection of E. coli are based on β-glucuronidase activity, using the fluorogenic substrate 4-methylumbelliferyl β-D-glucuronide (MUG). This study was conducted to determine whether β-glucuronidase negative E. coli were present in significant numbers in environmental waters. Two hundred and forty E. coli cultures were isolated from 12 water samples collected from different environmental sources. β-glucuronidase activity was determined using lauryl tryptose broth with MUG, EC broth with MUG, and the Autoanalysis Colilert (AC) procedure. The isolates were also evaluated by the standard EC broth gas fermentation method for fecal coliforms. The results confirm that assaying for the enzyme β-glucuronidase utilizing the MUG substrate is an accurate method for the detection of E. coli in environmental waters. Key words: Escherichia coli, β-glucuronidase, 4-methylumbelliferyl β-D-glucuronide, water.

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Śliżewska, K., A. Nowak, M. Piotrowska, Z. Żakowska, M. Gajęcka, Ł. Zielonka, and M. Gajęcki. "Cecal enzyme activity in gilts following experimentally induced Fusarium mycotoxicosis." Polish Journal of Veterinary Sciences 18, no. 1 (March 1, 2015): 191–97. http://dx.doi.org/10.1515/pjvs-2015-0024.

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AbstractThe objective of the presented study was to examine the influence ofFusariummycotoxins (zearalenone – ZEN and deoxynivalenol – DON), administered separately and in combination, on the activity of cecal enzymes (β-glucosidase and β-glucuronidase) in gilts which were fed fodder contaminated with these mycotoxins. The activity of β-glucosidase and β-glucuronidase varied in the range of 0.170-1.236 μmol · h−1· mg−1and 8.701-96.704 μmol · h−1· mg−1, respectively. In the first two weeks, the toxins had no significant effect on the activity of β-glucosidase and β-glucuronidase in the ascending and descending colon. After week 3 and later on, ZEN and DON administered as a mixture led to the highest increase in the activity of both enzymes. Administered separately, DON affected the activity of enzymes more than ZEN. From the third week of the experiment, an increase in the activity of CW β-glucosidase and β-glucuronidase was observed.

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Hattori, Jiro, Hélène Labbé, and Brian L. Miki. "Construction and expression of a metallothionein–β-glucuronidase gene fusion." Genome 37, no. 3 (June 1, 1994): 508–12. http://dx.doi.org/10.1139/g94-071.

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A gene fusion consisting of the Chinese hamster metallothionein II and β-glucuronidase coding regions was constructed. The fusion protein expressed in Escherichia coli retained cadmium-binding capacity and β-glucuronidase activity. When expressed from the constitutive 35S promoter in transgenic tobacco, the levels of 109Cd accumulation in leaves were reduced to about 70% of those in untransformed control plants. Metallothionin-pJ-glucuronidase did not sequester a significant proportion of the leaf 109Cd taken up through the roots in vitro and therefore a sink for Cd was not created.Key words: metallothionein–β-glucuronidase fusion, cadmium, transgenic plants.

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OKREND, ANITA J. G., BONNIE E. ROSE, and CHARLES P. LATTUADA. "Use of 5-Bromo-4-Chloro-3-lndoxyl-β-D-Glucuronide in MacConkey Sorbitol Agar to Aid in the Isolation of Escherichia coli 0157:H7 from Ground Beef." Journal of Food Protection 53, no. 11 (November 1, 1990): 941–43. http://dx.doi.org/10.4315/0362-028x-53.11.941.

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The addition of 5-bromo-4-chloro-3-indoxyl-β-D-glucuronide (BCIG) at the 0.1 g/L level, to MacConkey sorbitol agar (MSA) plates aided in the isolation of Escherichia coli 0157:H7 from raw ground beef samples by differentiating β-glucuronidase positive from β-glucuronidase negative colonies. E. coli 0157:H7 colonies, being sorbitol negative, β-glucuronidase negative, remained white, while sorbitol negative, β-glucuronidase positive colonies turned green to blue. Addition of BCIG to the MSA agar reduced the number of false suspect colonies picked from the primary plating medium by 36% when compared to MSA. E. coli 0157:H7 was isolated from 11 out of 12 inoculated meat samples (0.7 E. coli 0157:H7/g) using MSA-BCIG as compared to 8 out of 12 samples using MSA without BCIG.

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Campbell, M. A., C. S. Kinlaw, and D. B. Neale. "Expression of luciferase and β-glucuronidase in Pinusradiata suspension cells using electroporation and particle bombardment." Canadian Journal of Forest Research 22, no. 12 (December 1, 1992): 2014–18. http://dx.doi.org/10.1139/x92-265.

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The reporter gene β-glucuronidase, under the control of the 35S promoter from cauliflower mosaic virus, was introduced into a suspension-cultured cell line of Pinusradiata using electroporation and particle bombardment. Electroporation of suspension-derived protoplasts in the presence of pBI221 resulted in transient β-glucuronidase activity. Maximum levels of β-glucuronidase activity were obtained 24 h after electroporation using field strengths of 1000 V/cm but decreased to background levels within 48 h. This decrease corresponded to a drop in protoplast viability and metabolic activity, as determined by fluorescein diacetate staining and chlorophyll fluorescence. Electroporation of P. radiata protoplasts with a plasmid containing a firefly luciferase reporter gene driven by a 35S promoter resulted in expression levels that were 2–3.5 times that of background. Biolistic transfer of a β-glucuronidase coding sequence driven by a 35S promoter resulted in histochemically detectable β-glucuronidase activity in P. radiata suspension culture cells. Extracts from P. radiata suspension culture cells containing 800 μg soluble protein inhibited the β-glucuronidase activity of Escherichiacoli extracts by 50%. Aliquots of P. radiata extracts containing less than 100 μg of total soluble protein did not exhibit any inhibitory effect. These studies establish two different methods of gene transfer into a P. radiata cell line and will contribute to our ability to examine a variety of promoter types associated with transcriptional regulation in conifers.

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Sebastiano, Marisa, Marina D'Alessio, and Paolo Bazzicalupo. "β-GLUCURONIDASE MUTANTS OF THE NEMATODE CAENORHABDITIS ELEGANS." Genetics 112, no. 3 (March 1, 1986): 459–68. http://dx.doi.org/10.1093/genetics/112.3.459.

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ABSTRACT Using a screening procedure that is based on a histochemical stain for the enzyme β-glucuronidase, we have isolated several mutants of the nematode Caenorhabditis elegans affected in β-glucuronidase activity. All of the mutations fall into one complementation group and identify a new gene, gus-1, which has been mapped on the right arm of linkage group I (LG I), 1.1 map units to the left of unc-54. The mutants have no visible phenotype, and their viabilities and fertilities are unaffected. Linked revertants of two of the mutations have been isolated. They restore enzyme activity to almost wild-type levels; the β-glucuronidase that one of the revertants produces differs from that of the wild type. We propose that gus-1 is the structural locus for β-glucuronidase.

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George, Joseph. "Elevated serum β-glucuronidase reflects hepatic lysosomal fragility following toxic liver injury in rats." Biochemistry and Cell Biology 86, no. 3 (April 2008): 235–43. http://dx.doi.org/10.1139/o08-038.

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The level of serum β-glucuronidase increases in various pathological conditions, including liver disorders. The aim of this investigation was to study the changes in liver lysosomal membrane stability during experimentally induced hepatic fibrosis that may result in the elevation of serum β-glucuronidase. Liver injury was induced by intraperitoneal injections of N-nitrosodimethylamine (NDMA) in adult male albino rats over 3 weeks. The progression of fibrosis was evaluated histopathologically as well as by monitoring liver collagen content. Lipid peroxides and β-glucuronidase levels were measured in the liver homogenate and subcellular fractions on days 0, 7, 14, and 21 after the start of NDMA administration. Serum β-glucuronidase levels were also determined. A significant increase was observed in β-glucuronidase levels in the serum, liver homogenate, and subcellular fractions, but not in the nuclear fraction on days 7, 14, and 21 after the start of NDMA administration. Lipid peroxides also increased in the liver homogenate and the lysosomal fraction. The measurement of lysosomal membrane stability revealed a maximum lysosomal fragility on day 21 during NDMA-induced fibrosis. In vitro studies showed that NDMA has no significant effect on liver lysosomal membrane permeability. The results of this investigation demonstrated that lysosomal fragility increases during NDMA-induced hepatic fibrosis, which could be attributed to increased lipid peroxidation of lysosomal membrane. In this study, we also elucidated the mechanism of increased β-glucuronidase and other lysosomal glycohydrolases in the serum during hepatic fibrosis.

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Russell, W. M., and T. R. Klaenhammer. "Identification and Cloning of gusA, Encoding a New β-Glucuronidase from Lactobacillus gasseriADH." Applied and Environmental Microbiology 67, no. 3 (March 1, 2001): 1253–61. http://dx.doi.org/10.1128/aem.67.3.1253-1261.2001.

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ABSTRACT The gusA gene, encoding a new β-glucuronidase enzyme, has been cloned from Lactobacillus gasseri ADH. This is the first report of a β-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 β-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 β-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 β-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 β-glucuronidase activity and gusA homologs in other L. gasseri isolates but not in otherLactobacillus species tested.

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Gwynn, Babette, Kira Lueders, Mark S. Sands, and Edward H. Birkenmeier. "Intracisternal A-Particle Element Transposition into the Murine β-Glucuronidase Gene Correlates with Loss of Enzyme Activity: a New Model for β-Glucuronidase Deficiency in the C3H Mouse." Molecular and Cellular Biology 18, no. 11 (November 1, 1998): 6474–81. http://dx.doi.org/10.1128/mcb.18.11.6474.

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ABSTRACT The severity of human mucopolysaccharidosis type VII (MPS VII), or Sly syndrome, depends on the relative activity of the enzyme β-glucuronidase. Loss of β-glucuronidase activity can cause hydrops fetalis, with in utero or postnatal death of the patient. In this report, we show that β-glucuronidase activity is not detectable by a standard fluorometric assay in C3H/HeOuJ (C3H) mice homozygous for a new mutation, gusmps2J . Thesegusmps2J/gusmps2J mice are born and survive much longer than the previously characterized β-glucuronidase-null B6.C-H-2 bm1 /ByBir-gusmps (gusmps/gusmps ) mice. Northern blot analysis of liver fromgusmps2J/gusmps2J mice demonstrates a 750-bp reduction in size of β-glucuronidase mRNA. A 5.4-kb insertion in the Gus-sh nucleotide sequence from these mice was localized by Southern blot analysis to intron 8. The ends of the inserted sequences were cloned by inverse PCR and revealed an intracisternal A-particle (IAP) element inserted near the 3′ end of the intron. The sequence of the long terminal repeat (LTR) regions of the IAP most closely matches that of a composite LTR found in transposed IAPs previously identified in the C3H strain. The inserted IAP may contribute to diminished β-glucuronidase activity either by interfering with transcription or by destabilizing the message. The resulting phenotype is much less severe than that previously described in thegusmps/gusmps mouse and provides an opportunity to study MPS VII on a genetic background that clearly modulates disease severity.

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Phong, Nguyen Viet, Yan Zhao, Byung Sun Min, Seo Young Yang, and Jeong Ah Kim. "Inhibitory Activity of Bioactive Phloroglucinols from the Rhizomes of Dryopteris crassirhizoma on Escherichia coli β-Glucuronidase: Kinetic Analysis and Molecular Docking Studies." Metabolites 12, no. 10 (October 2, 2022): 938. http://dx.doi.org/10.3390/metabo12100938.

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Phloroglucinols—one of the major secondary metabolites in Dryopteris crassirhizoma—exhibit various pharmacological effects, such as antiviral, antioxidant, and antidiabetic activities. This study evaluated 30 phloroglucinols isolated from the rhizomes of D. crassirhizoma for their inhibitory activity on β-glucuronidase via in vitro assays. Among them, dimeric phloroglucinols 13–15 moderately inhibited β-glucuronidase, and trimeric phloroglucinols 26–28 showed strong inhibitory effects, with IC50 values ranging from 5.6 to 8.0 μM. Enzyme kinetic analysis confirmed all six active compounds to be in a competitive mode of inhibition. Molecular docking simulations revealed the key binding interactions with the active site of β-glucuronidase protein and the binding mechanisms of these active metabolites. Our results suggest that the rhizomes of D. crassirhizoma and trimeric compounds 26–28 may serve as potential candidates for discovering and developing new β-glucuronidase inhibitors.

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Vainstein, Alexander, Morly Fisher, and Meira Ziv. "Applicability of Reporter Genes to Carnation Transformation." HortScience 28, no. 11 (November 1993): 1122–24. http://dx.doi.org/10.21273/hortsci.28.11.1122.

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The applicability of β- glucuronidase and chloramphenicol acetyltransferase reporter genes to a carnation (Dianthus caryophyllus L.) transformation procedure, was analyzed. Transgenic tobacco (Nicotiana tabacum L.) plants expressing the respective reporter genes were prepared and used as the enzyme source. Carnation leaf extract strongly inhibited enzymatic activity of β- glucuronidase, but not that of chloramphenicol acetyltransferase. One or more carnation phenolic compounds, acting in a noncompetitive manner, is suggested as the cause of the observed inhibition of fluorometrically assayed β- glucuronidase activity. This inhibition was eliminated by treating the carnation leaf extract with polyvinylpolypyrrolidone.

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Marwani, Erly, Agustina Tangapo, and Fenny Martha Dwivany. "Agrobacterium-Mediated Stable Transformation of Medicinal Plant Andrographis paniculata Callus Expressing β-glucuronidase (GUS) Gene." Indonesian Journal of Biotechnology 18, no. 2 (November 9, 2015): 92. http://dx.doi.org/10.22146/ijbiotech.7873.

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This study was carried out to establish a stable genetic transformation in callus culture of Andrographispaniculata mediated by Agrobacterium tumefaciens. The leaf disks of A. paniculata were infected with A. tumefaciensLBA4404 carrying a binary vector pCAMBIA1304 that contain β-glucuronidase (GUS) and hygromycinphosphotransferase (hpt) genes. The infection was conducted by dipping method for one hour, followed byco-cultivation in the dark for three days. To examine transient GUS expression, the co-cultivated leaf disks wereassayed for β-glucuronidase activity and to obtain stable transformed callus, the co-cultivated leaf disks wereselected on the callus induction medium which contain 20 mg/l hygromycin for selection. The transformedcallus was periodically subcultured every three weeks into the fresh selection medium over the 15 weeksperiod. To test a stable transformation, the callus was subjected to PCR analysis for GUS gene detection. Theresults indicated that the co-cultivated leaf disks expressed GUS activity and proliferated to produce callus onthe selective medium. Analysis of PCR on the transformed callus indicated the presence 976 bp fragment thatconfi rmed the presence of β-glucuronidase gene. These fi ndings imply that the β-glucuronidase was stably integrated into A. paniculata callus culture.Keywords: Andrographis paniculata, Agrobacterium tumefaciens, andrographollide, transformed callus,β-glucuronidase gene.

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Beaud, Diane, Patrick Tailliez, and Jamila Anba-Mondoloni. "Genetic characterization of the β-glucuronidase enzyme from a human intestinal bacterium, Ruminococcus gnavus." Microbiology 151, no. 7 (July 1, 2005): 2323–30. http://dx.doi.org/10.1099/mic.0.27712-0.

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β-Glucuronidase activity (encoded by the gus gene) has been characterized for the first time from Ruminococcus gnavus E1, an anaerobic bacterium belonging to the dominant human gut microbiota. β-Glucuronidase activity plays a major role in the generation of toxic and carcinogenic metabolites in the large intestine, as well as in the absorption and enterohepatic circulation of many aglycone residues with protective effects, such as lignans, flavonoids, ceramide and glycyrrhetinic acid, that are liberated by the hydrolysis of the corresponding glucuronides. The complete nucleotide sequence of a 4537 bp DNA fragment containing the β-glucuronidase locus from R. gnavus E1 was determined. Five ORFs were detected on this fragment: three complete ORFs (ORF2, gus and ORF3) and two partial ORFs (ORF4 and ORF5). The products of ORF2 and ORF3 show strong similarities with many β-glucoside permeases of the phosphoenolpyruvate : β-glucoside phosphotransferase systems (PTSs), such as Escherichia coli BglC, Bacillus subtilis BglP and Bacillus halodurans PTS Enzyme II. The product of ORF5 presents strong similarities with the amino-terminal domain of Clostridium acetobutylicum β-glucosidase (bglA). The gus gene product presents similarities with several known β-glucuronidase enzymes, including those of Lactobacillus gasseri (69 %), E. coli (61 %), Clostridium perfringens (59 %) and Staphylococcus aureus (58 %). By complementing an E. coli strain in which the uidA gene encoding the enzyme was deleted, it was confirmed that the R. gnavus gus gene encodes the β-glucuronidase enzyme. Moreover, it was found that the gus gene was transcribed as part of an operon that includes ORF2, ORF3 and ORF5.

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Phong, Nguyen Viet, Byung Sun Min, Seo Young Yang, and Jeong Ah Kim. "Inhibitory Effect of Coumarins and Isocoumarins Isolated from the Stems and Branches of Acer mono Maxim. against Escherichia coli β-Glucuronidase." Applied Sciences 12, no. 20 (October 21, 2022): 10685. http://dx.doi.org/10.3390/app122010685.

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Abstract:

We isolated eight known secondary metabolites, including two isocoumarins and six coumarins, from the stems and branches of Acer mono Maxim. Their structures were confirmed using nuclear magnetic resonance spectroscopy and by comparing the data to published reports. The inhibitory effects of all compounds (1−8) on Escherichia coli β-glucuronidase were evaluated for the first time using in vitro assays. 3-(3,4-Dihydroxyphenyl)-8-hydroxyisocoumarin (1) displayed an inhibitory effect against β-glucuronidase (IC50 = 58.83 ± 1.36 μM). According to the findings of kinetic studies, compound 1 could function as a non-competitive inhibitor. Molecular docking indicated that compound 1 binds to the allosteric binding site of β-glucuronidase, and the results corroborated those from kinetic studies. Furthermore, molecular dynamics simulations of compound 1 were performed to identify the behavioral and dynamic properties of the protein–ligand complex. Our results reveal that compound 1 could be a lead metabolite for designing new β-glucuronidase inhibitors.

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Oh, Eun-Hee, Jung-Mi Park, Sang-Hee Kim, In-Gyu Song, Nam-Soo Han, and Hyang-Sik Yoon. "Biological Activities of Phellinus linteus Mycelium Culture with Cassiae Semen Extract on β-Glucuronidase Inhibitory Activity." Korean Journal of Food And Nutrition 25, no. 3 (September 30, 2012): 620–28. http://dx.doi.org/10.9799/ksfan.2012.25.3.620.

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Journal articles on the topic 'Β-Glucuronidases'

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