| pubmed-article:3606622 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3606622 | lifeskim:mentions | umls-concept:C0004594 | lld:lifeskim |
| pubmed-article:3606622 | lifeskim:mentions | umls-concept:C0003765 | lld:lifeskim |
| pubmed-article:3606622 | lifeskim:mentions | umls-concept:C0022917 | lld:lifeskim |
| pubmed-article:3606622 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:3606622 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:3606622 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3606622 | pubmed:dateCreated | 1987-8-27 | lld:pubmed |
| pubmed-article:3606622 | pubmed:abstractText | A variant of lactate dehydrogenase from Bacillus stearothermophilus has been engineered by site-directed mutagenesis in which an active-site arginine residue at position 171 in the protein sequence is replaced by lysine. Replacement of this arginine by lysine has no effect on co-enzyme binding, a relatively small effect on the rate of turnover of the enzyme, but causes a 2000-fold increase in the Michaelis constant for pyruvate, a 6000-fold increase in the dissociation constant for oxamate and results in a Michaelis constant for lactate which is too high to measure. The decrease in binding energy for these carboxylate-containing substrates caused by this mutation is very large, around 5.5 kcal.mol-1 and in part, is explained by the small increase in the distance of a lysine-substrate carboxylate interaction at this site and the absence of the additional hydrogen bond from a two-point arginine-carboxylate interaction. Consistent with this last observation, the ability of this mutant enzyme to stabilize an NAD+-sulphite compound in its active site (an alternative enzyme-substrate complex which does not involve bifurcated bonding to arginine) is only reduced 14-fold. | lld:pubmed |
| pubmed-article:3606622 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3606622 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3606622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3606622 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3606622 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:3606622 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:HolbrookJ JJJ | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:AtkinsonTT | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:ClarkeA RAR | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:HartK WKW | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:WigleyD BDB | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:ChiaW NWN | lld:pubmed |
| pubmed-article:3606622 | pubmed:author | pubmed-author:BarstowD ADA | lld:pubmed |
| pubmed-article:3606622 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3606622 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3606622 | pubmed:volume | 146 | lld:pubmed |
| pubmed-article:3606622 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3606622 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3606622 | pubmed:pagination | 346-53 | lld:pubmed |
| pubmed-article:3606622 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:3606622 | pubmed:meshHeading | pubmed-meshheading:3606622-... | lld:pubmed |
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| pubmed-article:3606622 | pubmed:meshHeading | pubmed-meshheading:3606622-... | lld:pubmed |
| pubmed-article:3606622 | pubmed:meshHeading | pubmed-meshheading:3606622-... | lld:pubmed |
| pubmed-article:3606622 | pubmed:meshHeading | pubmed-meshheading:3606622-... | lld:pubmed |
| pubmed-article:3606622 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3606622 | pubmed:articleTitle | The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase. | lld:pubmed |
| pubmed-article:3606622 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3606622 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3606622 | lld:pubmed |
