Chloramphenicol acetyltransferase active site
WebPseudomonas aeruginosa isolates are highly resistant to chloramphenicol (minimal inhibitory concentration, 100–1,000 μg/ml). Most of the strains tested produce the … WebAug 23, 1994 · The Carbonyl bandwidth in the wild-type complex is reduced by 33% compared to that for the complex with S148A, indicating restriction of carbonyl mobility and dispersion in the former, an observation consistent with the proposed hydrogen bond between the ester carbonyL and the hydroxyl group of Ser-148. Chloramphenicol …
Chloramphenicol acetyltransferase active site
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WebThe location of the cat gene within the PstI fragment was determined by Southern blotting with a cat consensus oligonucleotide corresponding to the expected amino acid sequence of the active site region of chloramphenicol acetyltransferase, and the direction of transcription was deduced from homology with the type I cat variant. WebJan 1, 2001 · Fully active chloramphenicol acetyltransferase represents 30-50% of the soluble protein component of cell-free extracts of E. coli containing the appropriate plasmids. ... Kleanthous C, Cullis PM, Shaw WV. 3-(Bromoacetyl)chloramphenicol, an active site directed inhibitor for chloramphenicol acetyltransferase. Biochemistry. 1985 Sep 24; …
WebFeb 22, 1991 · Site-directed replacement of Ser550 in the E2p subunit (LAT) of the pyruvate dehydrogenase complex of Escherichia coli, deemed to be equivalent to the active-site Ser148 of CAT, supported the CAT-based model of LAT catalysis. The effects of other substitutions were also consistent with the predicted similarity in catalytic mechanism … WebMar 22, 1996 · We report the cloning of a transcription-associated histone acetyltransferase type A (HAT A). This Tetrahymena enzyme is strikingly homologous to the yeast protein Gcn5, a putative transcriptional adaptor, and we demonstrate that recombinant Gcn5p possesses HAT activity. Both the ciliate enzyme and Gcn5p contain …
WebCornel Mülhardt, E.W. Beese M.D., in Molecular Biology and Genomics, 2007. Reporter Genes for Quanititative Evidence: Chloramphenicol Acetyltransferase. Chloramphenicol acetyltransferase (CAT) is the classic example among reporter genes. The enzyme catalyzes the transfer of an acetyl remnant of acetyl CoA to chloramphenicol.The cell … WebPseudomonas aeruginosa isolates are highly resistant to chloramphenicol (minimal inhibitory concentration, 100–1,000 μg/ml). Most of the strains tested produce the enzyme chloramphenicol acetyltransferase (CAT) while 15% do not produce the enzyme, although they are highly resistant to the drug. In an attempt to understand the resistance …
WebChloramphenicol O-Acetyltransferase / chemistry. Chloramphenicol O-Acetyltransferase / genetics. Chloramphenicol O-Acetyltransferase / metabolism*. Models, Molecular. Molecular Sequence Data. Mutagenesis, Site-Directed. Protein Conformation. Protein Engineering. X-Ray Diffraction / methods.
WebAug 24, 2024 · Acetyl-CoA is a reactive metabolite that non-productively hydrolyzes in a number of enzyme active sites on the crystallization time frame. In order to elucidate enzyme:acetyl-CoA interactions leading to catalysis, acetyl-CoA substrate analogs are needed. One possible analog for use in structural studies is acetyl-oxa(dethia)CoA … cannot fully bend kneeWebFeb 9, 2024 · The two active sites in the FabH homodimer appear to have negative cooperativity in the binding of and/or reaction with acetyl-CoA (Alhamadsheh et al., 2007). Once one FabH active site has formed the acyl-enzyme intermediate, there is a large decrease in the rate of acetylation of the second active site. cannot fully empty bowelsWebIn the active site of the peptidyl transferase, there is a water residue. When the tetrahedral intermediate is formed, the oxyanion now has a negative charge because the oxygen has one extra electron. The hydrogen on the water has a partial positive charge, which stabilizes the tetrahedral oxyanion intermediate. ... Chloramphenicol binds to ... cannot free up space on c driveWebChloramphenicol acetyltransferase [acetyl-CoA:chloramphenicol O3-acetyltransferase; EC 2.3.1.28] is the enzyme responsible for high-level bacterial resistance to the antibiotic … fkc 2 5/ 2-stf-5 08WebJun 25, 1991 · DOI: 10.1016/s0021-9258(18)99012-5 Corpus ID: 2619824; Stabilization of the imidazole ring of His-195 at the active site of chloramphenicol acetyltransferase. @article{Murray1991StabilizationOT, title={Stabilization of the imidazole ring of His-195 at the active site of chloramphenicol acetyltransferase.}, author={Iain A. Murray and … fkc 2.5/3-st-5.08WebChloramphenicol acetyltransferase (or CAT) is a bacterial enzyme (EC 2.3.1.28) that detoxifies the antibiotic chloramphenicol and is responsible for chloramphenicol resistance in bacteria. This enzyme covalently … fkc 2.5/14-st-5.08WebDec 1, 1990 · 1. The type III variant of chloramphenicol acetyltransferase (CATIII) is resistant to inactivation by ionizable modifying reagents such as 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and iodoacetate, whereas it is sensitive to inhibition by similar but uncharged reagents, including 4,4'-dithiodipyridine, methyl methanethiolsulphonate (MMTS) and … fkc220