| pubmed-article:19470521 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19470521 | lifeskim:mentions | umls-concept:C0050688 | lld:lifeskim |
| pubmed-article:19470521 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:19470521 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:19470521 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:19470521 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:19470521 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:19470521 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:19470521 | pubmed:dateCreated | 2009-8-27 | lld:pubmed |
| pubmed-article:19470521 | pubmed:abstractText | The interactions of acyl-CoA with medium-chain acyl-CoA dehydrogenases (MCADs) reconstituted with artificial FADs-i.e. 8-CN-, 7,8-Cl(2)-, 8-Cl-, 8-OCH(3)- and 8-NH(2)-FAD-were investigated by UV-visible absorption and FT-IR measurements. Although 8-NH(2)-FAD-MCAD did not oxidize acyl-CoA the wavelength of the absorption maximum of the flavin was altered by acyl-CoAs binding. Thus, 8-NH(2)-FAD-MCAD is one of the attractive materials for investigation of enzyme-substrate (ES) interaction in ES complex (the complex of oxidized MCAD with acyl-CoA). FT-IR difference spectra between non-labelled and [1-(13)C]-labelled acyl-CoA free in solution and bound to oxidized 8-NH(2)-FAD-MCAD were obtained. The broad 1668-cm(-1) band of free octanoyl-CoA assigned to the C(1) = O stretching vibration appeared as a sharp signal at 1626 cm(-1) in the case of the complex. The downward shift indicates a large polarization of C(1) = O, and the sharpness suggests that the orientation of the C(1) = O in the active-site cavity is fairly limited. The hydrogen-bond enthalpy change responsible for the polarization on the transfer of the substrate from aqueous solution to the active site of MCAD was estimated to be approximately 15 kcal/mol. The 1626-cm(-1) band is noticeably weakened in the case of acyl-CoA with acyl chains longer than C12 which are poor substrates for MCAD, suggesting that C(1) = O is likely to exist in multiple orientations in the active-site cavity, whence the band becomes obscured. A band identical to that of bound C8-CoA was observed in the case of C4-CoA which is a poor substrate, indicating the strong hydrogen bond at C(1) = O. | lld:pubmed |
| pubmed-article:19470521 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19470521 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19470521 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19470521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19470521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19470521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19470521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19470521 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19470521 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19470521 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:19470521 | pubmed:issn | 1756-2651 | lld:pubmed |
| pubmed-article:19470521 | pubmed:author | pubmed-author:SetoyamaChiak... | lld:pubmed |
| pubmed-article:19470521 | pubmed:author | pubmed-author:NishinaYasuzo... | lld:pubmed |
| pubmed-article:19470521 | pubmed:author | pubmed-author:TamaokiHaruhi... | lld:pubmed |
| pubmed-article:19470521 | pubmed:author | pubmed-author:ShigaKiyoshiK | lld:pubmed |
| pubmed-article:19470521 | pubmed:author | pubmed-author:MiuraRetsuR | lld:pubmed |
| pubmed-article:19470521 | pubmed:author | pubmed-author:SatoKyosukeK | lld:pubmed |
| pubmed-article:19470521 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19470521 | pubmed:volume | 146 | lld:pubmed |
| pubmed-article:19470521 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19470521 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19470521 | pubmed:pagination | 351-7 | lld:pubmed |
| pubmed-article:19470521 | pubmed:meshHeading | pubmed-meshheading:19470521... | lld:pubmed |
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| pubmed-article:19470521 | pubmed:meshHeading | pubmed-meshheading:19470521... | lld:pubmed |
| pubmed-article:19470521 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19470521 | pubmed:articleTitle | FT-IR spectroscopic studies on the molecular mechanism for substrate specificity/activation of medium-chain acyl-CoA dehydrogenase. | lld:pubmed |
| pubmed-article:19470521 | pubmed:affiliation | Department of Physiology, School of Health Sciences, Kumamoto University, Kuhonji, Kumamoto 862-0976, Japan. nishina@kumamoto-u.ac.jp | lld:pubmed |
| pubmed-article:19470521 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:397104 | entrezgene:pubmed | pubmed-article:19470521 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19470521 | lld:entrezgene |
