| pubmed-article:15579906 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15579906 | lifeskim:mentions | umls-concept:C0010654 | lld:lifeskim |
| pubmed-article:15579906 | lifeskim:mentions | umls-concept:C0079866 | lld:lifeskim |
| pubmed-article:15579906 | lifeskim:mentions | umls-concept:C1413689 | lld:lifeskim |
| pubmed-article:15579906 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:15579906 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:15579906 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:15579906 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15579906 | pubmed:dateCreated | 2005-2-7 | lld:pubmed |
| pubmed-article:15579906 | pubmed:abstractText | Carnitine palmitoyltransferase (CPT) I catalyzes the conversion of long-chain fatty acyl-CoAs to acyl carnitines in the presence of l-carnitine, a rate-limiting step in the transport of long-chain fatty acids from the cytoplasm to the mitochondrial matrix. To determine the role of the 15 cysteine residues in the heart/skeletal muscle isoform of CPTI (M-CPTI) on catalytic activity and malonyl-CoA sensitivity, we constructed a 6-residue N-terminal, a 9-residue C-terminal, and a 15-residue cysteineless M-CPTI by cysteine-scanning mutagenesis. Both the 9-residue C-terminal mutant enzyme and the complete 15-residue cysteineless mutant enzyme are inactive but that the 6-residue N-terminal cysteineless mutant enzyme had activity and malonyl-CoA sensitivity similar to those of wild-type M-CPTI. Mutation of each of the 9 C-terminal cysteines to alanine or serine identified a single residue, Cys-305, to be important for catalysis. Substitution of Cys-305 with Ala in the wild-type enzyme inactivated M-CPTI, and a single change of Ala-305 to Cys in the 9-residue C-terminal cysteineless mutant resulted in an 8-residue C-terminal cysteineless mutant enzyme that had activity and malonyl-CoA sensitivity similar to those of the wild type, suggesting that Cys-305 is the residue involved in catalysis. Sequence alignments of CPTI with the acyltransferase family of enzymes in the GenBank led to the identification of a putative catalytic triad in CPTI consisting of residues Cys-305, Asp-454, and His-473. Based on the mutagenesis and substrate labeling studies, we propose a mechanism for the acyltransferase activity of CPTI that uses a catalytic triad composed of Cys-305, His-473, and Asp-454 with Cys-305 serving as a probable nucleophile, thus acting as a site for covalent attachment of the acyl molecule and formation of a stable acyl-enzyme intermediate. This would in turn allow carnitine to act as a second nucleophile and complete the acyl transfer reaction. | lld:pubmed |
| pubmed-article:15579906 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15579906 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15579906 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15579906 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15579906 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15579906 | pubmed:author | pubmed-author:WoldegiorgisG... | lld:pubmed |
| pubmed-article:15579906 | pubmed:author | pubmed-author:ZhengGuoluG | lld:pubmed |
| pubmed-article:15579906 | pubmed:author | pubmed-author:LiuHongyanH | lld:pubmed |
| pubmed-article:15579906 | pubmed:author | pubmed-author:DaiJiaJ | lld:pubmed |
| pubmed-article:15579906 | pubmed:author | pubmed-author:TreberMichell... | lld:pubmed |
| pubmed-article:15579906 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15579906 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:15579906 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15579906 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15579906 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15579906 | pubmed:pagination | 4524-31 | lld:pubmed |
| pubmed-article:15579906 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15579906 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15579906 | pubmed:articleTitle | Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis. | lld:pubmed |
| pubmed-article:15579906 | pubmed:affiliation | Department of Environmental and Biomolecular Systems, OGI School of Science and Engineering, Oregon Health & Science University, Beaverton, Oregon 97006-8921, USA. | lld:pubmed |
| pubmed-article:15579906 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15579906 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:1375 | entrezgene:pubmed | pubmed-article:15579906 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:15579906 | lld:entrezgene |
