| http://purl.uniprot.org/citations/18305111 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18305111 | http://www.w3.org/2000/01/rdf-schema#comment | "Acyl-CoA synthetase, which is one of the acid-thiol ligases (EC 6.2.1), plays key roles in metabolic and regulatory processes. This enzyme forms a carbon-sulfur bond in the presence of ATP and Mg(2+), yielding acyl-CoA thioesters from the corresponding free acids and CoA. This enzyme belongs to the superfamily of adenylate-forming enzymes, whose three-dimensional structures are analogous to one another. We here discovered a new reaction while studying the short-chain acyl-CoA synthetase that we recently reported (Hashimoto, Y., Hosaka, H., Oinuma, K., Goda, M., Higashibata, H., and Kobayashi, M. (2005) J. Biol. Chem. 280, 8660-8667). When l-cysteine was used as a substrate instead of CoA, N-acyl-l-cysteine was surprisingly detected as a reaction product. This finding demonstrated that the enzyme formed a carbon-nitrogen bond (EC 6.3.1 acid-ammonia (or amide) ligase (amide synthase); EC 6.3.2 acid-amino acid ligase (peptide synthase)) comprising the amino group of the cysteine and the carboxyl group of the acid. N-Acyl-d-cysteine, N-acyl-dl-homocysteine, and N-acyl-l-cysteine methyl ester were also synthesized from the corresponding cysteine analog substrates by the enzyme. Furthermore, this unexpected enzyme activity was also observed for acetyl-CoA synthetase and firefly luciferase, indicating the generality of the new reaction in the superfamily of adenylate-forming enzymes."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m709654200"xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/author | "Kobayashi M."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/author | "Abe T."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/author | "Hashimoto Y."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/author | "Hosaka H."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/author | "Tomita-Yokotani K."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/pages | "11312-11321"xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/title | "Discovery of amide (peptide) bond synthetic activity in Acyl-CoA synthetase."xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://purl.uniprot.org/core/volume | "283"xsd:string |
| http://purl.uniprot.org/citations/18305111 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18305111 |
| http://purl.uniprot.org/citations/18305111 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18305111 |
| http://purl.uniprot.org/uniprot/P52910#attribution-4E66FF713B32DE625B0FA35A42D15A24 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/18305111 |
| http://purl.uniprot.org/uniprot/Q01574#attribution-4E66FF713B32DE625B0FA35A42D15A24 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/18305111 |
| http://purl.uniprot.org/uniprot/#_P52910-mappedCitation-18305111 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18305111 |
| http://purl.uniprot.org/uniprot/#_Q01574-mappedCitation-18305111 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/18305111 |
| http://purl.uniprot.org/uniprot/P52910 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/18305111 |
| http://purl.uniprot.org/uniprot/Q01574 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/18305111 |