Rhodococcus Erythropolis
Mostrando 25-36 de 58 artigos, teses e dissertações.
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25. Targeted Disruption of the kstD Gene Encoding a 3-Ketosteroid Δ1-Dehydrogenase Isoenzyme of Rhodococcus erythropolis Strain SQ1
Microbial phytosterol degradation is accompanied by the formation of steroid pathway intermediates, which are potential precursors in the synthesis of bioactive steroids. Degradation of these steroid intermediates is initiated by Δ1-dehydrogenation of the steroid ring structure. Characterization of a 2.9-kb DNA fragment of Rhodococcus erythropolis SQ1 revea
American Society for Microbiology.
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26. Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides.
An enantioselective amidase from Rhodococcus erythropolis MP50 was purified to homogeneity. The enzyme has a molecular weight of about 480,000 and is composed of identical subunits with molecular weights of about 61,000. The NH2-terminal amino acid sequence was significantly different from previously published sequences of bacterial amidases. The purified am
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27. Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP.
The biochemical characterization of the muconate and the chloromuconate cycloisomerases of the chlorophenol-utilizing Rhodococcus erythropolis strain 1CP previously indicated that efficient chloromuconate conversion among the gram-positive bacteria might have evolved independently of that among gram-negative bacteria. Based on sequences of the N terminus and
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28. A single cytochrome P-450 system is involved in degradation of the herbicides EPTC (S-ethyl dipropylthiocarbamate) and atrazine by Rhodococcus sp. strain NI86/21.
During atrazine degradation by Rhodococcus sp. strain N186/21, N-dealkylated metabolites and an hydroxyisopropyl derivative are produced. The cytochrome P-450 system that is involved in degradation of thiocarbamate herbicides by strain N186/21 (I. Nagy, G. Schoofs, F. Compernolle, P. Proost, J. Vanderleyden, and R. De Mot, J. Bacteriol. 177:676-687, 1995) is
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29. Synthesis of Imidazol-2-yl Amino Acids by Using Cells from Alkane-Oxidizing Bacteria
Sixty-one strains of alkane-oxidizing bacteria were tested for their ability to oxidize N-(2-hexylamino-4-phenylimidazol-1-yl)-acetamide to imidazol-2-yl amino acids applicable for pharmaceutical purposes. After growth with n-alkane, 15 strains formed different imidazol-2-yl amino acids identified by chemical structure analysis (mass and nuclear magnetic res
American Society for Microbiology.
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30. Cloning and Heterologous Expression of an Enantioselective Amidase from Rhodococcus erythropolis Strain MP50
The gene for an enantioselective amidase was cloned from Rhodococcus erythropolis MP50, which utilizes various aromatic nitriles via a nitrile hydratase/amidase system as nitrogen sources. The gene encoded a protein of 525 amino acids which corresponded to a protein with a molecular mass of 55.5 kDa. The deduced complete amino acid sequence showed homology t
American Society for Microbiology.
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31. Limonene-1,2-Epoxide Hydrolase from Rhodococcus erythropolis DCL14 Belongs to a Novel Class of Epoxide Hydrolases
An epoxide hydrolase from Rhodococcus erythropolis DCL14 catalyzes the hydrolysis of limonene-1,2-epoxide to limonene-1,2-diol. The enzyme is induced when R. erythropolis is grown on monoterpenes, reflecting its role in the limonene degradation pathway of this microorganism. Limonene-1,2-epoxide hydrolase was purified to homogeneity. It is a monomeric cytopl
American Society for Microbiology.
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32. Biochemical Identification and Biophysical Characterization of a Channel-Forming Protein from Rhodococcus erythropolis
Organic solvent extracts of whole cells of the gram-positive bacterium Rhodococcus erythropolis contain a channel-forming protein. It was identified by lipid bilayer experiments and purified to homogeneity by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). The pure protein had a rather low molecular mass of about 8.4 kDa,
American Society for Microbiology.
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33. Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an α/β hydrolase fold and act via a two-step reaction mechanism including an enzyme–substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropoli
Oxford University Press.
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34. High-performance liquid chromatography analysis of mycolic acids as an aid in laboratory identification of Rhodococcus and Nocardia species.
High-performance liquid chromatography analysis of the p-bromophenacyl esters of mycolic acids from whole organisms gave chromatographic patterns that were useful in differentiation of Rhodococcus and Nocardia species. Rhodococcus equi, R. erythropolis, and R. rhodochrous contained more-polar mycolic acids and were easily separated from the less-polar mycoli
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35. Rhodococcus erythropolis DCL14 Contains a Novel Degradation Pathway for Limonene
Strain DCL14, which is able to grow on limonene as a sole source of carbon and energy, was isolated from a freshwater sediment sample. This organism was identified as a strain of Rhodococcus erythropolis by chemotaxonomic and genetic studies. R. erythropolis DCL14 also assimilated the terpenes limonene-1,2-epoxide, limonene-1,2-diol, carveol, carvone, and (�
American Society for Microbiology.
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36. Genetic analysis of the dsz promoter and associated regulatory regions of Rhodococcus erythropolis IGTS8.
The dsz gene cluster of Rhodococcus erythropolis IGTS8 comprises three genes, dszA, dszB, and dszC, whose products are involved in the conversion of dibenzothiophene (DBT) to 2-hydroxybiphenyl and sulfite. This organism can use DBT as the sole sulfur source but not as a carbon source. Dsz activity is repressed by methionine, cysteine, Casamino Acids, and sul