| pubmed-article:6114098 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C1135183 | lld:lifeskim |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C0080103 | lld:lifeskim |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C2257525 | lld:lifeskim |
| pubmed-article:6114098 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:6114098 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:6114098 | pubmed:dateCreated | 1981-9-15 | lld:pubmed |
| pubmed-article:6114098 | pubmed:abstractText | Thiolase I (long chain 3-ketoacyl-CoA-specific) from porcine heart has been characterized kinetically. In the direction of acetoacetyl-CoA cleavage, a variety of thiols including CoASH show the same Vmax at saturating concentrations of acetoacetyl-CoA. At a constant overall velocity of acetoacetyl-CoA disappearance, one of the two acetyl groups from acetoacetyl-CoA will partition between CoASH and 2-mercaptoethanol at increasing 2-mercaptoethanol concentrations. These observations suggest rate-determining formation of an acetyl enzyme intermediate in the direction of acetoacetyl-CoA cleavage. In the direction of acetoacetyl-CoA formation from two molecules of acetyl-CoA, the Vmax of acetoacetyl-CoA formation is identical with the Vmax for an acetyl-CoA in equilibrium CoA isotope exchange reaction and the Vmax for an enzyme-catalyzed acetyl transfer reaction between acetyl-CoA and 2-mercaptoethanol. This suggests that in the direction of acetoacetyl-CoA synthesis, the acetyl transfer half-reaction is rate-limiting. The acetyl intermediate has been isolated and characterized. The equilibrium constant for acetyl enzyme formation from acetyl-CoA and free enzyme is 1 +/- 0.5 X 10(-2). The rate constant for spontaneous hydrolysis of the acetyl enzyme (2.6 X 10(-4) s-1) is a factor of 400 faster than the rate constant for acetyl-CoA hydrolysis under comparable conditions. The acetyl enzyme is thermodynamically and kinetically destabilized compared to acetyl-CoA. | lld:pubmed |
| pubmed-article:6114098 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6114098 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6114098 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6114098 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6114098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6114098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6114098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6114098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6114098 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6114098 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:6114098 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6114098 | pubmed:author | pubmed-author:GilbertH FHF | lld:pubmed |
| pubmed-article:6114098 | pubmed:author | pubmed-author:LennoxB JBJ | lld:pubmed |
| pubmed-article:6114098 | pubmed:author | pubmed-author:MossmanC DCD | lld:pubmed |
| pubmed-article:6114098 | pubmed:author | pubmed-author:CarleW CWC | lld:pubmed |
| pubmed-article:6114098 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6114098 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6114098 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:6114098 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6114098 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6114098 | pubmed:pagination | 7371-7 | lld:pubmed |
| pubmed-article:6114098 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6114098 | pubmed:meshHeading | pubmed-meshheading:6114098-... | lld:pubmed |
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| pubmed-article:6114098 | pubmed:meshHeading | pubmed-meshheading:6114098-... | lld:pubmed |
| pubmed-article:6114098 | pubmed:meshHeading | pubmed-meshheading:6114098-... | lld:pubmed |
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| pubmed-article:6114098 | pubmed:meshHeading | pubmed-meshheading:6114098-... | lld:pubmed |
| pubmed-article:6114098 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:6114098 | pubmed:articleTitle | The relation of acyl transfer to the overall reaction of thiolase I from porcine heart. | lld:pubmed |
| pubmed-article:6114098 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6114098 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6114098 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6114098 | lld:pubmed |
