Phosphotransferases
Mostrando 1-12 de 31 artigos, teses e dissertações.
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1. AMINOGLYCOSIDE RESISTANCE GENES IN Pseudomonas aeruginosa ISOLATES FROM CUMANA, VENEZUELA
The enzymatic modification of aminoglycosides by aminoglycoside-acetyltransferases (AAC), aminoglycoside-adenyltransferases (AAD), and aminoglycoside-phosphotransferases (APH), is the most common resistance mechanism in P. aeruginosa and these enzymes can be coded on mobile genetic elements that contribute to their dispersion. One hundred and thirty seven P.
Rev. Inst. Med. trop. S. Paulo. Publicado em: 22/03/2016
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2. Seleção de compostos como candidatos para a inibição da atividade de proteínas cinases humanas da família das Neks / Compound selection as candidates dor inhibition of kinase activity of human Neks
Cinases desempenham um papel importante na ativação de vias bioquímicas em células eucarióticas. Neks (NIMA related kinases) são uma família conservada de proteínas cinases relacionadas à progressão do ciclo celular e divisão celular, contendo em torno de 40% de identidade no domínio catalítico N-terminal com a proteína NIMA (Never in Mitosis,
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 14/05/2012
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3. Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases
Acetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP through crystallography. As we previously predicted, acetate kinase contains a core fold that is topologically identical to tha
American Society for Microbiology.
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4. Chromogenic Detection of Aminoglycoside Phosphotransferases
A coupled chromogenic reaction (based on an agar overlay combining NADH, pyruvate kinase, lactate dehydrogenase, phosphoenolpyruvate, ATP, and kanamycin sulfate with thiazolyl blue-phenazine methosulfate for detection of NADH consumption) was optimized for the detection of aminoglycoside phosphotransferases (APHs). When used after analytical isoelectrofocusi
American Society for Microbiology.
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5. Urkinase: Structure of Acetate Kinase, a Member of the ASKHA Superfamily of Phosphotransferases
American Society for Microbiology.
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6. Initial Characterization of Hexose and Hexitol Phosphoenolpyruvate-Dependent Phosphotransferases of Staphylococcus aureus
The phosphoenolpyruvate sugar phosphotransferases of Staphylococcus aureus were surveyed biochemically to determine substrate range, inducibility and constitutivity, and requirements for soluble sugar-specific proteins. The substrate range is similar to that of the phosphotransferases of enteric bacteria, but the staphylococcal mannose and sorbitol systems a
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7. Plasmid-mediated aminoglycoside phosphotransferases in Haemophilus ducreyi.
Three clinical isolates of Haemophilus ducreyi, representing at least two subtypes, were shown to be resistant to streptomycin and kanamycin. They also produced a beta-lactamase and chloramphenicol acetyltransferase and were resistant to tetracycline. In the three strains the resistance to both aminoglycoside antibiotics was encoded by a plasmid of ca. 4.7 k
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8. The Phosphotransferase System of Streptomyces coelicolor Is Biased for N-Acetylglucosamine Metabolism
Mutation of the crr-ptsI gene locus revealed that Streptomyces coelicolor uses the phosphotransferase system (PTS) for N-acetylglucosamine uptake. crr, ptsI, and ptsH, which encode the three general PTS phosphotransferases, are induced by N-acetylglucosamine but not by other PTS substrates. Thus, the S. coelicolor PTS is biased for N-acetylglucosamine utiliz
American Society for Microbiology.
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9. Mutations in the aph(2")-Ic Gene Are Responsible for Increased Levels of Aminoglycoside Resistance
Random PCR mutagenesis of the enterococcal aph(2")-Ic gene followed by selection for mutant enzymes that confer enhanced levels of aminoglycoside resistance resulted in mutants of APH(2")-Ic with His-258-Leu and Phe-108-Leu substitutions, all of which conferred rises in the MICs of several aminoglycosides. The mutated residues are located outside conserved r
American Society for Microbiology.
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10. Isolation of a gene encoding a novel spectinomycin phosphotransferase from Legionella pneumophila.
A gene capable of conferring spectinomycin resistance was isolated from Legionella pneumophila, the agent of Legionnaires' disease. The gene (aph) encoded a 36-kDa protein which has similarity to aminoglycoside phosphotransferases. Biochemical analysis confirmed that aph encodes a phosphotransferase which modifies spectinomycin but not hygromycin, kanamycin,
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11. Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis.
We report the cloning of the pykA and pykF genes from Escherichia coli, which code for the two pyruvate kinase isoenzymes (ATP:pyruvate 2-O-phosphotransferases; EC 2.7.1.40) in this microorganism. These genes were insertionally inactivated with antibiotic resistance markers and utilized to interrupt one or both pyk genes in the E. coli chromosome. With these
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12. Nucleotide sequence of a streptomycete aminoglycoside phosphotransferase gene and its relationship to phosphotransferases encoded by resistance plasmids.
The DNA sequence of an aminoglycoside phosphotransferase gene (aph) from Streptomyces fradiae ATCC 10745 (a neomycin producer) was determined. The gene was localized by in vitro subcloning and insertional inactivation. Molecular weight, amino acid composition, and amino-terminal analysis of the purified aph gene product confirmed the accuracy and position of