| pubmed-article:238842 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C0022192 | lld:lifeskim |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C0037874 | lld:lifeskim |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:238842 | lifeskim:mentions | umls-concept:C0041131 | lld:lifeskim |
| pubmed-article:238842 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:238842 | pubmed:dateCreated | 1975-11-8 | lld:pubmed |
| pubmed-article:238842 | pubmed:abstractText | Isoleucyl-tRNA formation catalysed by isoleucine: tRNA ligase is stimulated by both Mg2+ and spermine in the pH-range 7.0 to 8.0 at 310 K. At low [Mg2+] the acceleration caused by both cations together exceeds the sum of their individual effects. 2. The spermine-stimulated reaction has a steeper temperature-dependence than reaction in the presence of Mg2+. Two phases in the kinetics of isoleucyl-tRNA formation are detected in the presence of Mg2+ plus or minus spermine, but only a single step is observed in the presence of spermine alone. Thus the rate-limiting steps under normal assay conditions are different for the two cations. 3. Enzyme-bound isoleucyl-AMP can be formed in the absence of Mg-2+ and plus or minus spermine. 4. It is concluded that there is no evidence for cation-dependent differences in the reaction mechanism of isoleucine: tRNA ligase, though there are certainly differences in the relative rates of some of the individual steps. | lld:pubmed |
| pubmed-article:238842 | pubmed:language | eng | lld:pubmed |
| pubmed-article:238842 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:238842 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:238842 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:238842 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:238842 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:238842 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:238842 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:238842 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:238842 | pubmed:month | May | lld:pubmed |
| pubmed-article:238842 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:238842 | pubmed:author | pubmed-author:CarrA CAC | lld:pubmed |
| pubmed-article:238842 | pubmed:author | pubmed-author:IgloiG LGL | lld:pubmed |
| pubmed-article:238842 | pubmed:author | pubmed-author:PenzerG RGR | lld:pubmed |
| pubmed-article:238842 | pubmed:author | pubmed-author:PlumbridgeJ... | lld:pubmed |
| pubmed-article:238842 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:238842 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:238842 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:238842 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:238842 | pubmed:pagination | 169-73 | lld:pubmed |
| pubmed-article:238842 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-H... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-M... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-T... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-K... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-E... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-I... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-S... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-L... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-R... | lld:pubmed |
| pubmed-article:238842 | pubmed:meshHeading | pubmed-meshheading:238842-E... | lld:pubmed |
| pubmed-article:238842 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:238842 | pubmed:articleTitle | The effects of spermine and Mg2+ on the catalytic mechanism of isoleucine: tRNA ligase. | lld:pubmed |
| pubmed-article:238842 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:238842 | lld:pubmed |
