| pubmed-article:10092596 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10092596 | lifeskim:mentions | umls-concept:C0389003 | lld:lifeskim |
| pubmed-article:10092596 | lifeskim:mentions | umls-concept:C1151518 | lld:lifeskim |
| pubmed-article:10092596 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:10092596 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:10092596 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:10092596 | pubmed:dateCreated | 1999-4-27 | lld:pubmed |
| pubmed-article:10092596 | pubmed:abstractText | Prostaglandin H synthase (PGHS) is a self-activating and self-inactivating enzyme. Both the peroxidase and cyclooxygenase activities have a limited number of catalytic turnovers. Sequential stopped-flow measurements were used to analyze the kinetics of PGHS-1 peroxidase self-inactivation during reaction with several different hydroperoxides. The inactivation followed single exponential kinetics, with a first-order rate constant of 0.2-0.5 s-1 at 24 degrees C. This rate was independent of the peroxide species and concentration used, strongly suggesting that the self-inactivation process originates after formation of Compound I and probably with Intermediate II, which contains an oxyferryl heme and a tyrosyl radical. Kinetic scan and rapid scan experiments were used to monitor the heme changes during the inactivation process. The results from both experiments converged to a simple, linear, two-step mechanism in which Intermediate II is first converted in a faster step (0.5-2 s-1) to a new compound, Intermediate III, which undergoes a subsequent slower (0.01-0.05 s-1) transition to a terminal species. Rapid-quench and high pressure liquid chromatography analysis indicated that Intermediate III likely retains an intact heme group that is not covalently linked with the PGHS-1 protein. | lld:pubmed |
| pubmed-article:10092596 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10092596 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10092596 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10092596 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10092596 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10092596 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10092596 | pubmed:author | pubmed-author:OsawaYY | lld:pubmed |
| pubmed-article:10092596 | pubmed:author | pubmed-author:WeiCC | lld:pubmed |
| pubmed-article:10092596 | pubmed:author | pubmed-author:WuGG | lld:pubmed |
| pubmed-article:10092596 | pubmed:author | pubmed-author:KulmaczR JRJ | lld:pubmed |
| pubmed-article:10092596 | pubmed:author | pubmed-author:SYTZFF | lld:pubmed |
| pubmed-article:10092596 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10092596 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:10092596 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10092596 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10092596 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10092596 | pubmed:pagination | 9231-7 | lld:pubmed |
| pubmed-article:10092596 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
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| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
| pubmed-article:10092596 | pubmed:meshHeading | pubmed-meshheading:10092596... | lld:pubmed |
| pubmed-article:10092596 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10092596 | pubmed:articleTitle | A mechanistic study of self-inactivation of the peroxidase activity in prostaglandin H synthase-1. | lld:pubmed |
| pubmed-article:10092596 | pubmed:affiliation | Division of Hematology, Department of Internal Medicine, University of Texas Health Science Center, Houston, Texas 77030, USA. | lld:pubmed |
| pubmed-article:10092596 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10092596 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10092596 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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