| pubmed-article:18061544 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18061544 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:18061544 | lifeskim:mentions | umls-concept:C0050688 | lld:lifeskim |
| pubmed-article:18061544 | lifeskim:mentions | umls-concept:C1151759 | lld:lifeskim |
| pubmed-article:18061544 | lifeskim:mentions | umls-concept:C1706701 | lld:lifeskim |
| pubmed-article:18061544 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:18061544 | pubmed:dateCreated | 2007-12-17 | lld:pubmed |
| pubmed-article:18061544 | pubmed:abstractText | Medium-chain acyl-CoA dehydrogenase (MCAD) and acyl-CoA oxidase (ACO) are key enzymes catalyzing the rate-determining step for the beta-oxidation of fatty acids. Tyr375 of MCAD is conserved in all acyl-CoA dehydrogenases and is an important residue for substrate binding. Four Tyr375 variant enzymes of rat liver MCAD were obtained through site-directed mutagenesis. Y375K was found to have intrinsic acyl-CoA oxidase activity, which was confirmed using HPLC analysis, while the wild-type and other Tyr375 variant enzymes did not show detectable oxidase activity. The kinetic parameters for the oxidase activity of Y375K variant enzyme were determined to be k(cat) of 320+/-80 h(-1) and K(M) of 30+/-15 microM using hexanoyl-CoA as the substrate. The oxidase activity of Y375K increased more than 200 times compared with that reported for the MCAD wild-type enzyme from mammalian sources. Molecular modeling study shows that the solvent accessible area for Y375K variant enzyme is wider than that of the wild-type enzyme, which indicates that Tyr375 may function as a switch against solvent accession. The mutation of this residue to Lys375 allows molecular oxygen to enter into the catalytic site serving as the electron acceptor for the reduced FAD cofactor. | lld:pubmed |
| pubmed-article:18061544 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18061544 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18061544 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18061544 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:18061544 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:18061544 | pubmed:author | pubmed-author:DingLiL | lld:pubmed |
| pubmed-article:18061544 | pubmed:author | pubmed-author:WuLongL | lld:pubmed |
| pubmed-article:18061544 | pubmed:author | pubmed-author:ZengJiaJ | lld:pubmed |
| pubmed-article:18061544 | pubmed:author | pubmed-author:LiuYuandongY | lld:pubmed |
| pubmed-article:18061544 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18061544 | pubmed:volume | 1774 | lld:pubmed |
| pubmed-article:18061544 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18061544 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18061544 | pubmed:pagination | 1628-34 | lld:pubmed |
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| pubmed-article:18061544 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:18061544 | pubmed:articleTitle | Mutation of Tyr375 to Lys375 allows medium-chain acyl-CoA dehydrogenase to acquire acyl-CoA oxidase activity. | lld:pubmed |
| pubmed-article:18061544 | pubmed:affiliation | Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, PR China; Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha 410083, PR China. | lld:pubmed |
| pubmed-article:18061544 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18061544 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:24158 | entrezgene:pubmed | pubmed-article:18061544 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18061544 | lld:entrezgene |
