Disease relevance of Acylate

• An Ehrlich ascites extract was shown in these in vitro studies to acylate Escherichia coli tRNA with 13 amino acids, and the ascites extract was used in place of the corresponding 13 E. coli aminoacyl-tRNA synthetases [1].
• MICs of a set of cephalosporins against a variety of gram-positive and gram-negative pathogens showed no strong correlations with the rate at which these inhibitors acylate or are deacylated by beta-lactam-sensitive DD-peptidases excreted by Streptomyces sp. strain R61 and Actinomadura sp. strain R39 [2].
• When expressed in Spodoptera frugiperda cells by a baculovirus vector, the hemagglutinin of fowl plague virus has been found to contain palmitic acid in covalent hydroxylamine-sensitive linkage, indicating that these cells have the capacity to acylate foreign proteins at cysteine residues [3].

High impact information on Acylate

• All three mischarging mutant enzymes still retain a certain degree of tRNA specificity; in vivo they acylate supE glutaminyl tRNA (tRNA(Gln] and supF tRNA(Tyr) but not a number of other suppressor tRNA's. These genetic experiments define two positions in GlnRS where amino acid substitution results in a relaxed specificity of tRNA discrimination [4].
• Although the synthetases are widely conserved through evolution, aminoacylation of a given tRNA is often system specific-a synthetase from one source will not acylate its cognate tRNA from another [5].
• (iii) Mitochondria from a mutant with a disrupted chromosomal copy of MSD1 are unable to acylate mitochondrial aspartyl-tRNA [6].
• When B. subtilis, A. fulgidus, and human TrpRS were used to acylate these tRNA(Trp), two distinct preference profiles regarding the discriminator base of different tRNA(Trp) substrates were found: G>A>U>C for B. subtilis TrpRS, and A>C>U>G for A. fulgidus and human TrpRS [7].
• In contrast, a discriminating AspRS cannot acylate tRNA(Asn) [8].

Chemical compound and disease context of Acylate

• When Escherichia coli aminoacyl-tRNA synthetases were used to acylate S. antibioticus tRNA's, it was observed that, per absorbance unit of tRNA, the tRNA's from 48-h cells had a lower ability to accept the amino acids, leucine, serine, pheynlalanine, methionine, and valine than did the tRNA's from 12-h cells [9].
• An enzyme preparation able to acylate the hydroxyl group at C-3 of the lactone ring of spiramycin was obtained from the spiramycin-producing strain, Streptomyces ambofaciens ISP-5053 [10].

Biological context of Acylate

• We did not detect HlyC in cell lysates from hlyC mutants with different abilities to acylate pro-HlyA, suggesting that the degradation of HlyC is not related to the HlyA acylation process [11].
• We postulate that the SLC1 suppressor allele encodes a variant enzyme with an altered substrate specificity that enables it to use a C26 in place of a C16/18 fatty acid precursor to acylate the sn-2 position of inositol-containing glycerolipids [12].
• Extracts of strains harboring msbB+ bearing plasmids acylate (Kdo)2-(lauroyl)-lipid IVA very rapidly compared with wild type [13].
• This gene confers a respiratory competent phenotype and restores the mutant's ability to acylate the mitochondrial lysine tRNA [14].
• This hypothesis explains both the relative potencies of these compounds and their differential abilities to acylate the TBPS binding site [15].

Anatomical context of Acylate

• Resting human neutrophils acylate 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (1-O-alkyl-2-lyso-GPC; lyso-PAF) specifically with arachidonate (AA); upon stimulation, however, the specificity is lost and other fatty acid residues are added [16].
• Rabbit alveolar macrophage microsomes were found to acylate 1-[3H]alkyl-glycero-3-phosphocholine (GPC) (lyso platelet-activating factor) in the absence of any cofactors, indicating the presence of transacylation activity [17].
• These findings indicate that mucosal PLA2 activity increases during intestinal maturation and that the mucosa acquires the ability to acylate and deacylate lysoPC when it is 'closed' to macromolecules [18].
• In contrast to microsomes from rat liver, about 70% of the product with the 1- and 2-monooleoylglycerol ethers was triradylglycerol, suggesting that the diacylglycerol acyltransferase from chick liver can acylate acyl, alkylglycerols [19].
• Diacylglycerol acyltransferase and lysophosphatidylcholine acyltransferase had similar dependences on palmitoyl-CoA in both liver and fibroblasts; thus it did not appear that acyl-CoAs, when present at low concentrations, would be preferentially used to acylate lysophospholipids [20].

Associations of Acylate with other chemical compounds

• Repeated rounds of DNA shuffling and oligonucleotide-directed mutagenesis followed by genetic selection resulted in mutant GlnRS enzymes that efficiently acylate the engineered tRNA with glutamine in vitro [21].
• Azapeptide p-nitrophenyl esters acylate both HL and PP elastase to form stable acylenzymes, which can be used for crystallographic studies [22].
• Extracts of a temperature-sensitive firA mutant, RL-25, were assayed for their ability to acylate UDP-GlcNAc, using a coupled assay [23].
• These inhibitors (GR157368, GR166081, GR167088, and GR179849) are representatives of a series utilizing a novel 5, 5-trans-lactone template to specifically acylate Ser195 of thrombin, resulting in an acyl complex [24].
• Although the observed metaphit concentrations during the first 4 h are high enough to acylate receptors, no firm evidence for acylation was found for most of the examined receptors [25].

Gene context of Acylate

• Amino-acylation of wild-type mitochondrial tRNAs with a mitochondrial extract from mst1 mutants fail to acylate tRNAThr1 (anticodon: 3'-GAU-5') but show normal acylation of tRNAThr2 (anticodon: 3'-UGU-5') [26].
• E. coli ArgRS can acylate only its cognate E. coli tRNA [27].
• Single-chain TPA (recSCTPA) has been found to acylate more slowly than its two-chain counterpart and to exhibit a higher degree of turnover of the acyl-enzyme with this reagent [28].
• Lecithin-cholesterol acyltransferase (LCAT) in human plasma has been shown to acylate lysolecithin to lecithin in presence of low density lipoprotein (LDL) [29].
• An enzymic mechanism for the conversion of OA and DTX-2 seems to be implicated in some kind of detoxification process because the percentage of esters increases with the toxin amount ingested by the bivalve and there is some degree of selectivity as DTX-2 seems more difficult to acylate [30].

Analytical, diagnostic and therapeutic context of Acylate

• The use of HPLC has established that chickens possess unexpected metabolic abilities to acylate, deacylate, reduce, and oxidize carotenoids [31].

References