| pubmed-article:6721853 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0022023 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0034340 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0244104 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
| pubmed-article:6721853 | lifeskim:mentions | umls-concept:C0068323 | lld:lifeskim |
| pubmed-article:6721853 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:6721853 | pubmed:dateCreated | 1984-6-18 | lld:pubmed |
| pubmed-article:6721853 | pubmed:abstractText | The enzyme-[14C] carboxybiotin complex of sheep liver pyruvate carboxylase was isolated and the reaction between this and pyruvate was studied by using the quenched-flow rapid-reaction technique. At 0.5 degrees C the reaction was 80% complete within 180 ms. The reaction was monophasic and obeyed pseudo-first-order kinetics. Increasing concentrations of Mg2+ caused a decrease in the magnitude of the observed pseudo-first-order rate constant. Throughout the carboxylation of pyruvate, the rate-limiting step of the reaction occurred after the dissociation of carboxybiotin from the first sub-site, whereas in the slow phase of the reaction with 2-oxobutyrate this dissociation is the rate-limiting step. It is possible, from the reaction scheme proposed, that the inhibition of overall enzymic activity by high concentrations of Mg2+ could be caused by the transfer of the carboxy group from biotin to pyruvate becoming rate-limiting. The efficacy of a substrate as a signal for the movement of carboxybiotin from the first sub-site is reflected by the amount that the effective affinity of the enzyme- carboxybiotin complex for Mg2+ is lowered. In the presence of the substrates tested, the affinities of the carboxybiotin complex can be arranged in order of increasing magnitude, i.e.: (formula; see text). The kinetics of the decay of the enzyme-[14C] carboxybiotin complex at 0 degree C in the absence of substrates are similar to the reaction with pyruvate except that the carboxybiotin is also unstable in the first sub-site, to some degree. This similarity allows for the proposal of a general scheme for the decarboxylation of the enzyme- carboxybiotin complex in the presence or in the absence of substrates. | lld:pubmed |
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| pubmed-article:6721853 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6721853 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6721853 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6721853 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6721853 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6721853 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:6721853 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6721853 | pubmed:author | pubmed-author:KeechD BDB | lld:pubmed |
| pubmed-article:6721853 | pubmed:author | pubmed-author:WallaceJ CJC | lld:pubmed |
| pubmed-article:6721853 | pubmed:author | pubmed-author:AttwoodP VPV | lld:pubmed |
| pubmed-article:6721853 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6721853 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:6721853 | pubmed:volume | 219 | lld:pubmed |
| pubmed-article:6721853 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6721853 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6721853 | pubmed:pagination | 243-51 | lld:pubmed |
| pubmed-article:6721853 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:meshHeading | pubmed-meshheading:6721853-... | lld:pubmed |
| pubmed-article:6721853 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6721853 | pubmed:articleTitle | The carboxybiotin complex of pyruvate carboxylase. A kinetic analysis of the effects of Mg2+ ions on its stability and on its reaction with pyruvate. | lld:pubmed |
| pubmed-article:6721853 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6721853 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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