| http://purl.uniprot.org/citations/15823031 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15823031 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/15823031 | http://www.w3.org/2000/01/rdf-schema#comment | "L-Carnitine (R-[-]-3-hydroxy-4-trimethylaminobutyrate) is found in both eukaryotic and prokaryotic cells and participates in diverse processes including long-chain fatty-acid transport and osmoprotection. The enzyme crotonobetainyl/gamma-butyrobetainyl-CoA:carnitine CoA-transferase (CaiB; E.C. 2.8.3.-) catalyzes the first step in carnitine metabolism, leading to the final product gamma-butyrobetaine. The crystal structures of Escherichia coli apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, have been determined and refined to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The monomer and dimer resemble those of formyl-CoA transferase from Oxalobacter formigenes, as well as E. coli YfdW, a putative type-III CoA transferase of unknown function. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. While the location of cofactor binding is similar in the three proteins, the specific CoA-protein interactions vary somewhat between CaiB, formyl-CoA transferase, and YfdW. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB. The observed carnitinyl-CoA product in crystals of the CaiB Asp169Ala mutant cocrystallized with crotonoyl-CoA and carnitine could result from (i) a catalytic mechanism involving a ternary enzyme-substrate complex, independent of a covalent anhydride intermediate with Asp169, (ii) a spontaneous reaction of the substrates in solution, followed by binding to the enzyme, or (iii) an involvement of another residue substituting functionally for Asp169, such as Glu23."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi047656f"xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/author | "Cygler M."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/author | "Li Y."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/author | "Matte A."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/author | "Rangarajan E.S."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/author | "Iannuzzi P."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/pages | "5728-5738"xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/title | "Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA."xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://purl.uniprot.org/core/volume | "44"xsd:string |
| http://purl.uniprot.org/citations/15823031 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15823031 |
| http://purl.uniprot.org/citations/15823031 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15823031 |
| http://purl.uniprot.org/citations/15823031 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15823031 |
| http://purl.uniprot.org/citations/15823031 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15823031 |
| http://purl.uniprot.org/enzyme/2.8.3.21 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/15823031 |
| http://purl.uniprot.org/uniprot/#_P31572-mappedCitation-15823031 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15823031 |
| http://purl.uniprot.org/uniprot/P31572 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15823031 |