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

Inhibition of a tartrate-resistant acid phosphatase (ACP) from Leishmania donovani and the tartrate-sensitive ACP from human seminal fluid (prostatic ACP) was examined using a series of 13 molybdate-containing heteropolyanions. The heteropolyanions were divided into four groups based on the number of molybdenum atoms they contain: Group I, Mo4; Group II, Mo6-8; Group III, Mo12; Group IV, Mo18. Two of the four groups, those consisting of compounds that contain either an Mo4 unit or an Mo18 unit with a heteroatom in the central cavity, were potent inhibitors and exhibited the highest degree of selectivity against the leishmanial and seminal fluid ACPs. The inhibition of prostatic ACP by complex E2 could be completely reversed by dialysis. Little inhibition of the acid phosphatase, beta-glucuronidase, or alpha-mannosidase from human spleen was observed with complexes B' and E2. For the seminal fluid phosphatase, the Ki values obtained with arsenate and vanadate depended markedly on pH, suggesting that, unlike most other phosphatases, the conformation of the inhibitor binding site on human seminal fluid ACP is pH-dependent. Results of competition experiments performed with various inhibitor pairs indicated that complex D2 binds to the active site of prostatic ACP while complex M binds at some site on the enzyme that affects the active site. Binding of complex M also modifies the affinity of the enzyme for other inhibitors such as vanadate. The potency of several heteropolyanion complexes and their selective inhibition of pathophysiologically significant acid phosphatases indicate that these compounds may have value as tools for study of the structure and function of this class of enzyme and perhaps in the therapy of human disease.
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PMID:Inhibition of human seminal fluid and Leishmania donovani phosphatases by molybdate heteropolyanions. 199 14

The nitrate reductase (NR) gene niaA of the oomycete Phytophthora infestans was selected from a gene library by heterologous hybridization. NiaA occurs as a single-copy gene ant its expression is regulated by the nitrogen source. The nucleotide sequence of niaA was determined and comparison of the deduced amino-acid sequence of 902 residues with NRs of higher fungi and plants revealed a significant homology, particularly within the three cofactor-binding domains for molybdenum, heme and FAD. The P. infestans niaA gene was used as a model gene to test whether oomycete genes are functional in the ascomycete Aspergillus nidulans, a fungus which is highly accessible for molecular genetic studies. The complete niaA gene was stably integrated into the genome of a nia- deletion mutant of A. nidulans. However, transformants containing one or more copies of the niaA gene were not able to complement the nia- mutant. This suggests that there is no functional expression of the introduced niaA gene in A. nidulans. In addition, the activity of two other oomycete gene promoters was analyzed in a transient expression assay. Plasmids containing chimaeric genes with the promoter of the P. infestans ubiquitin gene ubi3R, or the Bremia lactucae ham34 gene, fused to the coding sequence of the Escherichia coli beta-glucuronidase (GUS) reporter gene, were transferred to A. nidulans protoplasts. No significant GUS activity was detectable indicating that the ubi3R and ham34 promoters are not active in A. nidulans. Apparently, the regulatory sequences which are sufficient for gene activation in oomycetes are not functional in the ascomycete A. nidulans.
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PMID:NiaA, the structural nitrate reductase gene of Phytophthora infestans: isolation, characterization and expression analysis in Aspergillus nidulans. 761 59

Sulfite oxidase (SO), one of the known molybdenum co-factor-containing enzymes, plays important roles in diverse metabolic processes such as sulfur detoxification and purine catabolism in mammals. But much less is known about the expression and regulatory characterization of sulfite oxidase gene in higher plants. In this report, expression of Arabidopsis SO is characterized in detail by semi-quantitative RT-PCR and histochemical staining. The results showed that the transcripts of AtSO were predominantly detected in Arabidopsis aerial tissues including stems, young leaves, young inflorescences and immature siliques at higher level, but in roots with a lower level. To monitor AtSO expression in plant, the promoter region containing a 1 562-bp genomic sequence from AtSO was isolated and analyzed using methods of bioinformatics. Basing on the distribution of beta-glucuronidase (GUS) activities shown by histochemical staining in transgenic Arabidopsis plants harboring the promoter-uidA fusion construct, it can be concluded that AtSO is expressed mainly in the green tissues/organs in a light-dependent way. In addition, its expression is up-regulated during sulfite treatment. The information from this study may provide useful clue for further functional analysis of plant SO homologs during light-induced development of leaf tissue and/or excessive sulfite/SO(2) gas stresses in higher plants.
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PMID:Isolation and functional analysis of sulfite oxidase gene AtSO promoter from Arabidopsis thaliana. 1796 39