Zobrazeno 1 - 10 of 47 pro vyhledávání: '"W V, Shaw"'
2
Crystallization and preliminary diffraction studies of NodL, a rhizobial O -acetyl-transferase involved in the host-specific nodulation of legume roots
Autor: Steven M. Dunn, J. A. Downie, W. V. Shaw, Peter C. E. Moody
Publikováno v: Protein Science. 5:538-541
The NodL specified O-acetyltransferase from the microbial symbiont Rhizobium leguminosarum has been over-expressed in Escherichia coli and purified using affinity-elution dye chromatography as the key step. The protein has been crystallized at 20 deg
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e32b00240b5298e6d54fd8c382e758c5
https://doi.org/10.1002/pro.5560050318
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3
The pKa of the catalytic histidine residue of chloramphenicol acetyltransferase
Autor: W V Shaw, A Lewendon
Publikováno v: Biochemical Journal. 290:15-19
A catalytically essential histidine residue (His-195) of chloramphenicol acetyltransferase (CAT) acts as a general base in catalysis, abstracting a proton from the primary hydroxy group of chloramphenicol. The pKa of His-195 has been determined from
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87c2331787498e342e94b6c82ffff7f0
https://doi.org/10.1042/bj2900015
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4
Some experiments on the Intravascular use of Antiseptics
Autor: W. V. Shaw
Publikováno v: The Journal of hygiene. 3(2)
The prominence given to the intravascular use of antiseptics has hardly been in accord with the results achieved by this method.The injection of formalin in various amounts and strengths has been given an extended trial in the treatment of pulmonary
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daf6ff0c5e81a80227d51103c38204a5
https://pubmed.ncbi.nlm.nih.gov/20474166
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5
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
Autor: T J Close, W V Shaw, I A Murray, J V Martinez-Suarez
Publikováno v: Biochemical Journal. 272:505-510
Sensitivity of enzymes to inhibition by thiol-reactive reagents is often presented as evidence for the possible involvement of cysteine residues in substrate binding and catalysis or to highlight possible important differences in structure and mechan
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0078e10152c14f772dcdcf8dda0f6781
https://doi.org/10.1042/bj2720505
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6
Inactivation of chloramphenicol by O-phosphorylation. A novel resistance mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer
Autor: R H, Mosher, D J, Camp, K, Yang, M P, Brown, W V, Shaw, L C, Vining
Publikováno v: The Journal of biological chemistry. 270(45)
Plasmid pJV4, containing a 2.4-kilobase pair insert of genomic DNA from the chloramphenicol (Cm) producer Streptomyces venezuelae ISP5230, confers resistance when introduced by transformation into the Cm-sensitive host Streptomyces lividans M252 (Mos
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b3af8939ea8e89d31f70f338b5108fa4
https://pubmed.ncbi.nlm.nih.gov/7592948
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7
Transition state stabilization by chloramphenicol acetyltransferase. Role of a water molecule bound to threonine 174
Autor: A, Lewendon, W V, Shaw
Publikováno v: The Journal of biological chemistry. 268(28)
The structure of the type III variant of chloramphenicol acetyltransferase reveals that Thr-174, a conserved residue, is hydrogen-bonded to a bound water molecule (water 252). Modeling studies (P. C. E. Moody and A. G. W. Leslie, unpublished data) su
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4a5316990d2604899a33284d0231874c
https://pubmed.ncbi.nlm.nih.gov/8407936
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8
Analysis of the binding of 1,3-diacetylchloramphenicol to chloramphenicol acetyltransferase by isotope-edited 1H NMR and site-directed mutagenesis
Autor: J P, Derrick, L Y, Lian, G C, Roberts, W V, Shaw
Publikováno v: Biochemistry. 31(35)
The binary complex of diacetylchloramphenicol and chloramphenicol acetyltransferase (CAT) has been studied by a combination of isotope-edited 1H NMR spectroscopy and site-directed mutagenesis. One-dimensional HMQC spectra of the complex between 1,3-[
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::04a7e15b34bf8a2e346a29e9c136106a
https://pubmed.ncbi.nlm.nih.gov/1525158
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9
Acetyl coenzyme A binding by chloramphenicol acetyltransferase. Hydrophobic determinants of recognition and catalysis
Autor: P J, Day, W V, Shaw
Publikováno v: The Journal of biological chemistry. 267(8)
The preponderance of nonpolar contacts between CoA and chloramphenicol acetyltransferase in the high resolution structure of the binary complex prompted a study of selected hydrophobic residues by site-directed mutagenesis and steady-state kinetic an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0b2d1e950571e4e3e39f82227f84c5b3
https://pubmed.ncbi.nlm.nih.gov/1544895
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10
Chemical anatomy of antibiotic resistance: chloramphenicol acetyltransferase
Autor: W V, Shaw
Publikováno v: Science progress. 76(301-302 Pt)
The evolution of mechanisms of resistance to natural antimicrobial substances (antibiotics) was almost certainly concurrent with the development in microorganisms of the ability to synthesise such agents. Of the several general strategies adopted by
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::fab54092cafe0194df8037cba489aa77
https://pubmed.ncbi.nlm.nih.gov/1364583
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