| pubmed-article:15035657 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0020281 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0023749 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0027078 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C1521828 | lld:lifeskim |
| pubmed-article:15035657 | lifeskim:mentions | umls-concept:C0680977 | lld:lifeskim |
| pubmed-article:15035657 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:15035657 | pubmed:dateCreated | 2004-6-30 | lld:pubmed |
| pubmed-article:15035657 | pubmed:abstractText | Mb (myoglobin) plus H2O2 catalyses the oxidation of various substrates via a peroxidase-like activity. A Y103F (Tyr103-->Phe) variant of human Mb has been constructed to assess the effect of exchanging an electron-rich oxidizable amino acid on the peroxidase activity of human Mb. Steady-state analyses of reaction mixtures containing Y103F Mb, purified linoleic acid and H2O2 revealed a lower total yield of lipid oxidation products than mixtures containing the wild-type protein, consistent with the reported decrease in the rate constant for reaction of Y103F Mb with H2O2 [Witting, Mauk and Lay (2002) Biochemistry 41, 11495-11503]. Irrespective of the Mb employed, lipid oxidation yielded 9(R/S)-HODE [9(R,S)-hydroxy-10E,12Z-octadecadienoic acid] in preference to 13(R/S)-HODE [13(R,S)-hydroxy-9Z,11E-octadecadienoic acid], while 9- and 13-keto-octadecadienoic acid were formed in trace amounts. However, lipid oxidation by the Y103F variant of Mb proceeded with a lower V(max) value and an increased K(m) value relative to the wild-type control. Consistent with the increased K(m), the product distribution from reactions with Y103F Mb showed decreased selectivity compared with the wild-type protein, as judged by the decreased yield of 9(S)-relative to 9(R)-HODE. Together, these data verify that Tyr103 plays a significant role in substrate binding and orientation in the haem pocket of human Mb. Also, the midpoint potential for the Fe(III)/(II) one-electron reduction was shifted slightly, but significantly, to a higher potential, confirming the importance of Tyr103 to the hydrogen-bonding network involving residues that line the haem crevice of human Mb. | lld:pubmed |
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| pubmed-article:15035657 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15035657 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15035657 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15035657 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15035657 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15035657 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15035657 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:15035657 | pubmed:author | pubmed-author:StockerRoland... | lld:pubmed |
| pubmed-article:15035657 | pubmed:author | pubmed-author:WittingPaul... | lld:pubmed |
| pubmed-article:15035657 | pubmed:author | pubmed-author:LayPeter APA | lld:pubmed |
| pubmed-article:15035657 | pubmed:author | pubmed-author:RaynerBenjami... | lld:pubmed |
| pubmed-article:15035657 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15035657 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15035657 | pubmed:volume | 381 | lld:pubmed |
| pubmed-article:15035657 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15035657 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15035657 | pubmed:pagination | 365-72 | lld:pubmed |
| pubmed-article:15035657 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:15035657 | pubmed:meshHeading | pubmed-meshheading:15035657... | lld:pubmed |
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| pubmed-article:15035657 | pubmed:meshHeading | pubmed-meshheading:15035657... | lld:pubmed |
| pubmed-article:15035657 | pubmed:meshHeading | pubmed-meshheading:15035657... | lld:pubmed |
| pubmed-article:15035657 | pubmed:meshHeading | pubmed-meshheading:15035657... | lld:pubmed |
| pubmed-article:15035657 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15035657 | pubmed:articleTitle | Regio- and stereo-chemical oxidation of linoleic acid by human myoglobin and hydrogen peroxide: Tyr(103) affects rate and product distribution. | lld:pubmed |
| pubmed-article:15035657 | pubmed:affiliation | Vascular Biology Group, ANZAC Research Institute, Hospital Road, Concord Repatriation General Hospital, Concord, NSW 2139, Australia. | lld:pubmed |
| pubmed-article:15035657 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15035657 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15035657 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15035657 | lld:pubmed |
