Search Results - "Shaw, W. V"

O-acetyltransferases for chloramphenicol and other natural products by MURRAY, I. A, SHAW, W. V

“…The range of enzymatic mechanisms by which bacteria inactivate biologically active molecules is limited by two kinds of constraint, namely, the…”
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Structure of chloramphenicol acetyltransferase at 1.75-A resolution by LESLIE, A. G. W, MOODY, P. C. E, SHAW, W. V

“…Chloramphenicol acetyltransferase [acetyl-CoA:chloramphenicol O3-acetyltransferase; EC 2.3.1.28] is the enzyme responsible for high-level bacterial resistance…”
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In vitro studies of the initiation of staphylococcal plasmid replication. Specificity of RepD for its origin (oriD) and characterization of the Rep-ori tyrosyl ester intermediate by THOMAS, C. D, BALSON, D. F, SHAW, W. V

“…Several staphylococcal plasmids from different incompatibility (inc) groups which replicate by a rolling circle mechanism each specify a replication initiator…”
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Chloramphenicol Resistance in Meningococci by Shaw, William V

“…The familiar triad of pathogens responsible for most cases of bacterial meningitis was first shown to yield to treatment with β-lactam antibiotics and…”
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Transition state stabilization by chloramphenicol acetyltransferase. Role of a water molecule bound to threonine 174 by LEWENDON, A, SHAW, W. V

“…The structure of the type III variant of chloramphenicol acetyltransferase reveals that Thr-174, a conserved residue, is hydrogen-bonded to a bound water…”
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Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: Evidence for a general base role for glutamate by Lewendon, Ann, Murray, Iain A, Shaw, William V, Gibbs, Michael R, Leslie, Andrew G. W

“…The imidazole N epsilon 2 of His-195 plays an essential part in the proposed general base mechanism of chloramphenicol acetyltransferase (CAT), hydrogen…”
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Protein engineering: the design, synthesis and characterization of factitious proteins by Shaw, W.V

“…A review…”
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Nucleotide sequences of genes encoding the type II chloramphenicol acetyltransferases of Escherichia coli and Haemophilus influenzae, which are sensitive to inhibition by thiol-reactive reagents by MURRAY, I. A, MARTINEZ-SUAREZ, J. V, CLOSE, T. J, SHAW, W. V

“…Sensitivity of enzymes to inhibition by thiol-reactive reagents is often presented as evidence for the possible involvement of cysteine residues in substrate…”
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Purification and Characterization of Phosphopantetheine Adenylyltransferase from Escherichia coli by Geerlof, Arie, Lewendon, Ann, Shaw, William V.

“…Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in coenzyme A (CoA) biosynthesis: the reversible adenylation of…”
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Acetyl coenzyme A binding by chloramphenicol acetyltransferase. Hydrophobic determinants of recognition and catalysis by DAY, P. J, SHAW, W. V

“…The preponderance of nonpolar contacts between CoA and chloramphenicol acetyltransferase in the high resolution structure of the binary complex prompted a…”
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Elimination of a reactive thiol group from the active site of chloramphenicol acetyltransferase by LEWENDON, A, SHAW, W. V

“…1. The type III variant of chloramphenicol acetyltransferase (CATIII) is resistant to inactivation by ionizable modifying reagents such as…”
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The Conformation of Coenzyme A Bound to Chloramphenicol Acetyltransferase Determined by Transferred NOE Experiments by Barsukov, I.L., Lian, L.-Y., Ellis, J., Sze, K.-H., Shaw, W.V., Roberts, G.C.K.

“…The conformation of coenzyme A bound to chloramphenicol acetyltrans ferase has been studied in solution by NMR methods. Transferred nuclear Overhauser…”
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The use of synthetic oligonucleotides with universal templates for rapid DNA sequencing: results with staphylococcal replicon pC221 by Brenner, D.G., Shaw, W.V.

“…A rapid sequencing strategy has been devised and applied to determine the complete nucleotide sequence (4555 bp) of Staphylococcus aureus plasmid pC221. The…”
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Stabilization of the imidazole ring of His-195 at the active site of chloramphenicol acetyltransferase by MURRAY, I. A, LEWENDON, A, SHAW, W. V

“…The imidazole of His-195 plays an essential role in the proposed general base mechanism of chloramphenicol acetyltransferase (CAT). The structure of the binary…”
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Analysis of the mechanism of chloramphenicol acetyltransferase by steady-state kinetics. Evidence for a ternary-complex mechanism by Kleanthous, C, Shaw, W V

“…The mechanism of the enzymic reaction responsible for chloramphenicol resistance in bacteria was examined by steady-state kinetic methods. The forward reaction…”
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Inducible plasmid-determined resistance to arsenate, arsenite, and antimony (III) in escherichia coli and Staphylococcus aureus by Silver, S, Budd, K, Leahy, K M, Shaw, W V, Hammond, D, Novick, R P, Willsky, G R, Malamy, M H, Rosenberg, H

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Nucleotide sequence of the chloramphenicol acetyltransferase gene of Streptomyces acrimycini by Murray, I A, Gil, J A, Hopwood, D A, Shaw, W V

“…The nucleotide sequence of a gene (cat) encoding chloramphenicol acetyltransferase (CAT) in Streptomyces acrimycini was determined. The predicted amino acid…”
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Nucleotide sequence analysis and overexpression of the gene encoding a type III chloramphenicol acetyltransferase by Murray, I A, Hawkins, A R, Keyte, J W, Shaw, W V

“…The gene catIII, encoding a type III enterobacterial chloramphenicol acetyltransferase, was cloned from the transmissible plasmid R387 into pBR322 and…”
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Primary structure of a chloramphenicol acetyltransferase specified by R plasmids by Shaw, W. V, Packman, L. C, Burleigh, B. D, Dell, A, Morris, H. R, Hartley, B. S

“…Naturally occurring isolates of chloramphenicol-resistant bacteria commonly synthesise chloramphenicol acetyltransferase (EC 2.3.28; CAT) in amounts which are…”
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Substrate binding to chloramphenicol acetyltransferase: evidence for negative cooperativity from equilibrium and kinetic constants for binary and ternary complexes by Ellis, Jacqueline, Bagshaw, Clive R, Shaw, William V

“…Chloramphenicol acetyltransferase (CAT) catalyzes the acetyl-CoA-dependent acetylation of chloramphenicol by a ternary complex mechanism with a rapid…”
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