| pubmed-article:11113461 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11113461 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:11113461 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:11113461 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:11113461 | lifeskim:mentions | umls-concept:C0534137 | lld:lifeskim |
| pubmed-article:11113461 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:11113461 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11113461 | pubmed:dateCreated | 2000-12-26 | lld:pubmed |
| pubmed-article:11113461 | pubmed:abstractText | Bacillus megaterium P450 BM3 is a fatty acid hydroxylase with selectivity for long chain substrates (C(12)-C(20)). Binding or activity with substrates of chain length <C(12) has not been reported. Rational mutagenesis was used to re-design the enzyme to encourage binding of short chain fatty acids (C(4)-C(10)). We show that wild-type P450 BM3 has activity and weak affinity for substrates as short as butyrate (C(4)). However, turnover/binding of short chain substrates is dramatically increased by introducing a novel substrate carboxylate binding site close to the heme. Mutant L181K shows catalytic efficiency (k(cat)/K(M)) increased >13-fold with butyrate, while the L75T/L181K double mutant has k(cat)/K(M) increased >15-fold with hexanoate and binding (K(d)) improved >28-fold for butyrate. Removing the arginine 47/lysine 51 carboxylate binding motif at the mouth of the active site disfavours binding of all fatty acids, indicating its importance in the initial recognition of substrates. | lld:pubmed |
| pubmed-article:11113461 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11113461 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11113461 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11113461 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11113461 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:ChapmanS KSK | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:ReidG AGA | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:CheungYY | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:MunroA WAW | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:HuVV | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:MurdochJJ | lld:pubmed |
| pubmed-article:11113461 | pubmed:author | pubmed-author:MilesC SCS | lld:pubmed |
| pubmed-article:11113461 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11113461 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:11113461 | pubmed:volume | 486 | lld:pubmed |
| pubmed-article:11113461 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11113461 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11113461 | pubmed:pagination | 173-7 | lld:pubmed |
| pubmed-article:11113461 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
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| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
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| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:meshHeading | pubmed-meshheading:11113461... | lld:pubmed |
| pubmed-article:11113461 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11113461 | pubmed:articleTitle | Rational re-design of the substrate binding site of flavocytochrome P450 BM3. | lld:pubmed |
| pubmed-article:11113461 | pubmed:affiliation | Department of Chemistry, University of Edinburgh, Edinburgh, UK. | lld:pubmed |
| pubmed-article:11113461 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11113461 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11113461 | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11113461 | lld:pubmed |
