• We have identified a cytosolic acyl-CoA binding protein, with highly conserved amino acid residues and a typical acyl-CoA binding domain in N. caninum . (biomedcentral.com)
  • This enzyme covalently attaches an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. (wikipedia.org)
  • Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase , acetyl-CoA acyltransferase , or beta-ketothiolase is an enzyme that in humans is encoded by the HADHB gene . (wikidoc.org)
  • An enzyme that catalyzes the transfer of acetyl groups from ACETYL-COA to arylamines. (wakehealth.edu)
  • An enzyme that catalyzes reversibly the conversion of palmitoyl-CoA to palmitoylcarnitine in the inner mitochondrial membrane. (lookformedical.com)
  • Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. (wikipedia.org)
  • [4] Trifunctional protein deficiency is characterized by decreased activity of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD), long-chain enoyl-CoA hydratase, and long-chain thiolase. (wikidoc.org)
  • The NcACBP recombinant protein was able to specifically bind acyl-CoA esters in vitro . (biomedcentral.com)
  • As a result, three different a-keto acids are produced and are oxidized using a common branched-chain a-keto acid dehydrogenase, yielding the three different CoA derivatives. (drugbank.com)
  • The HADHB protein catalyzes the final step of beta-oxidation, in which 3-ketoacyl CoA is cleaved by the thiol group of another molecule of Coenzyme A . The thiol is inserted between C-2 and C-3, which yields an acetyl CoA molecule and an acyl CoA molecule, which is two carbons shorter. (wikidoc.org)
  • Lipid synthesis requires bulk carbon skeleton acyl-CoAs, the transport of which depends on the acyl-CoA binding protein (ACBP). (biomedcentral.com)
  • Before entering lipid synthesis pathways, different kinds of acyl-CoA transporters which acts as the major carrier of acyl-CoAs, such as fatty acid binding protein (FABP), sterol carrier protein 2 (SCP2) and acyl-CoA-binding protein (ACBP), would activate and convert fatty acids to fatty acyl-CoA esters via a reaction catalyzed by fatty acyl-CoA synthetase and transported to various metabolic locations [ 11 ]. (biomedcentral.com)
  • CAT activity is determined by looking for the acetylated forms of chloramphenicol, which have a significantly increased migration rate as compared to the unacetylated form. (wikipedia.org)
  • DEP modified two histidine residues, one within the chloramphenicol binding site and one outside the substrate binding sites. (figshare.com)
  • In the binary complex with CoA, the hydroxyl group of Ser 558 is hydrogen bonded to the nitrogen atom of one of the two peptide-like units of the substrate. (rcsb.org)
  • Recently the mitochondrial fatty acid synthesis pathway (mtFAS) has been identified as a mechanism to regulate mitochondrial respiratory chain (RC) function to meet the substrate availability (acetyl-CoA) to tricarboxylic acid cycle 4 , 5 . (nature.com)
  • The acetyl-S-CoA analogues, acetonyl-S-CoA and methyl-S-CoA, were synthesised and characterized. (figshare.com)
  • Analogues of chloramphenicol: circular dichroism spectra, inhibition of ribosomal peptidyltransferase, and possible mechanism of action. (medchemexpress.com)
  • Chloramphenicol was able to protect against the loss of activity, supporting the hypothesis that a reactive sulphydryl group existed near or in the chloramphenicol binding site. (figshare.com)
  • This fact supports the indication, derived from the similarity with chloramphenicol acetyl transferase, that the histidine side chain acts as general-base catalyst in the deprotonation of the reactive thiol of CoA. (rcsb.org)
  • In this abortive ternary complex, CoA adopts a helical conformation with two intramolecular hydrogen bonds and the reactive sulfur of the pantetheine arm positioned 12 A away from the active site residues involved in the transferase reaction. (rcsb.org)
  • Chloramphenicol binds in a deep pocket located at the boundary between adjacent subunits of the trimer, such that the majority of residues forming the binding pocket belong to one subunit while the catalytically essential histidine belongs to the adjacent subunit. (wikipedia.org)
  • Since it was not possible to inactivate the C. glutamicum gene, the gene most likely encodes a subunit of the essential acetyl-CoA carboxylase, which catalyzes the committed step in fatty acid synthesis. (uni-bielefeld.de)
  • Many high-value products, such as isoprenoids, butanol, and polyketides, are derived from the intermediate acetyl-CoA, a key compound connecting the glycolysis and the tricarboxylic acid (TCA) cycle [ 10 ]. (biomedcentral.com)
  • P. putida , like many other bacteria grown on glycolytic carbon sources, produces acetyl-CoA through pyruvate decarboxylation. (biomedcentral.com)
  • marismortui, in which acetyl-CoA is oxidized to glyoxylate via methylaspartate as key intermediate (Khomyakova et al. (casr-signal.com)
  • The structure of CATIII reveals insight into the catalytic mechanism, with one active site of the trimer having relatively clear electron density for AcOCoA and chloramphenicol and the other active sites having weaker density for AcOCoA. (nih.gov)
  • Quite unexpectedly, the structure at 2.6-A resolution of a ternary complex in which CoA and Lip(SH)2 are simultaneously bound to E2pCD reveals that CoA has an alternative, nonproductive binding mode. (rcsb.org)
  • Thus, CoA itself is involved in keeping the Ser hydroxyl group in the proper position for transition-state stabilization. (rcsb.org)
  • One possible analog for use in structural studies is acetyl-oxa(dethia)CoA (AcOCoA), in which the thioester S atom of CoA is replaced by an O atom. (nih.gov)
  • CoA-transferase family III [Interproscan]. (ntu.edu.sg)
  • CAT activity is determined by looking for the acetylated forms of chloramphenicol, which have a significantly increased migration rate as compared to the unacetylated form. (wikipedia.org)