Disease relevance of ECs2831

• In Escherichia coli, acetyl phosphate can be formed from acetyl-CoA via the phosphotransacetylase (phosphate acetyltransferase; acetyl-CoA:orthophosphate acetyltransferase, EC 2.3.1.8) reaction and from acetate (plus ATP) via the acetate kinase (ATP:acetate phosphotransferase, EC 2.7.2.1) reaction [1].
• Identification of the satA gene encoding a streptogramin A acetyltransferase in Enterococcus faecium BM4145 [2].
• Cloning and characterization of a 3-N-aminoglycoside acetyltransferase gene, aac(3)-Ib, from Pseudomonas aeruginosa [3].
• Analysis of the deduced amino acid sequences indicated that the proteins belonged to a subfamily of 6'-aminoglycoside acetyltransferase type I enzymes from gram-negative bacteria [4].
• Variant Salmonella genomic island 1 antibiotic resistance gene cluster containing a novel 3'-N-aminoglycoside acetyltransferase gene cassette, aac(3)-Id, in Salmonella enterica serovar newport [5].

High impact information on ECs2831

• We describe reduced susceptibility to ciprofloxacin in clinical bacterial isolates conferred by a variant of the gene encoding aminoglycoside acetyltransferase AAC(6')-Ib [6].
• The nature of the recognition of acetyl-lysine by the P/CAF bromodomain is similar to that of acetyl-CoA by histone acetyltransferase [7].
• The C-terminal half of the molecule contains the acetyltransferase active site and the binding sites for E1, E3 and other E2 subunits [8].
• The deduced amino acid sequence contains the experimentally determined amino acid sequences of the amino terminus and two internal peptide fragments of the acetyltransferase [9].
• Chloramphenicol acetyltransferase [acetyl-CoA:chloramphenicol O3-acetyltransferase; EC 2.3.1.28] is the enzyme responsible for high-level bacterial resistance to the antibiotic chloramphenicol [10].

Chemical compound and disease context of ECs2831

• However, gene expression in Escherichia coli and enzymatic analysis showed that the MPR1 gene encodes a novel AZC acetyltransferase, by which L-proline itself and other L-proline analogues are not acetylated [11].
• The multiple-antibiotic resistance (mar) locus (min 34) regulates a resistance to chloramphenicol in Escherichia coli that does not involve acetyltransferase [12].
• We overexpressed Mat1 in Escherichia coli and demonstrated that this enzyme acts as an acetyl coenzyme A-dependent acetyltransferase [13].
• The oat2 gene, located in the clavulanic acid gene cluster in Streptomyces clavuligerus, is similar to argJ, which encodes N-acetylornithine:glutamic acid acetyltransferase activity [14].
• Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes [15].

Biological context of ECs2831

• A 537-base cDNA encoding a portion of Saccharomyces cerevisiae dihydrolipoamide acetyltransferase (acetyl-CoA:dihydrolipoamide S-acetyltransferase, EC 2.3.1.12) was isolated from a lambda gt11 yeast cDNA library by immunoscreening [9].
• It is shown that the acetyltransferase activity of the full-length protein is abolished once trapped within heterotrimers formed in presence of the truncated protein, suggesting that this enzyme activity absolutely requires a trimeric organization and that the catalytic site involves regions of contact between adjacent monomers [16].
• The accompanying reductive acetylation of the lipoyl group attached to the dihydrolipoyl acetyltransferase (E2) component involves weak, transient but specific interactions between E1 and the lipoyl domain of the E2 polypeptide chain [17].
• The aacC1 gene encoding the 3-N-aminoglycoside acetyltransferase [AAC(3)-I] was cloned from enteric plasmid pJR88, and its deoxyribonucleotide sequence was determined [18].
• This enzyme is unique in that it is composed of two separable modification domains, and although a number of studies have been conducted on the acetyltransferase and phosphotransferase activities in isolation, little is known about the role and impact of domain interactions on antibiotic resistance [19].

Anatomical context of ECs2831

• PAF activation of the acetyltransferase and PAF synthesis required intact neutrophils as they did not occur in cells broken by sonication [20].
• Escherichia coli alkaline phosphatase, which greatly decreased the activity of the acetyltransferase in spleen microsomes, had little or no effect on the basal or PAF-induced neutrophil acetyltransferase [20].
• Biochemical studies proved that chloramphenicol is not modified by an acetyltransferase or any other enzyme and that ribosomes of the resistant strain are sensitive to chloramphenicol [21].
• High acetyltransferase activity, however, was obtained when the fusion protein was expressed in the cytosol [22].

Associations of ECs2831 with chemical compounds

• Within 2 min of stimulation of neutrophils with 10(-6) M PAF, the 7-fold increase in acetyltransferase activity was coincident with substantial PAF synthesis (as measured by [3H]acetate incorporation into PAF), which was 14% of the PAF synthesis induced by the Ca2+ ionophore A23187 at 10(-5) M [20].
• Assembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex [23].
• These results strongly support the view that the three long (alanine + proline)-rich regions of the dihydrolipoyl acetyltransferase chains are exposed to solvent and enjoy substantial conformational flexibility in the enzyme complex [24].
• GAT was shown to be a trimeric acetyltransferase by cross-linking with dimethyl suberimidate [25].
• The biosynthesis of diacetamidobacillosamine is anticipated to involve a sugar nucleotide C6 dehydratase, a C4 aminotransferase and an acetyltransferase [26].

Analytical, diagnostic and therapeutic context of ECs2831

• Immunoblotting (Western) analysis revealed that the 50 kDa DAC acetyltransferase showed high protein levels in A. chrysogenum cultures at 72 and 96 h and decreased sharply thereafter, but in all cases no detectable processing of the enzyme into subunits was found [27].
• Multiplex PCR assays showed that every gentamicin-resistant isolate carried one of these acetyltransferase genes [28].
• Expression, purification and crystallization of enterococcus faecium streptogramin A acetyltransferase [29].
• The purification (126 fold) of the acetyltransferase was achieved by (NH4)2SO4 precipitation, DEAE chromatography and affinity chromatography [30].

References