| pubmed-article:1208211 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1208211 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:1208211 | lifeskim:mentions | umls-concept:C0035727 | lld:lifeskim |
| pubmed-article:1208211 | lifeskim:mentions | umls-concept:C0036001 | lld:lifeskim |
| pubmed-article:1208211 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:1208211 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:1208211 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:1208211 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:1208211 | pubmed:dateCreated | 1976-3-30 | lld:pubmed |
| pubmed-article:1208211 | pubmed:abstractText | Three tRNA methyltransferases from rat liver have been fractionated and purified greater than 100-fold. These enzymes have been examined for their sensitivity to inhibition by S-adenosylhomocysteine (SAH). The methyltransferase which forms m2-guanine in the region between the dihydrouridine loop and the acceptor stem of tRNA (m2-guanine methyltransferase I) is least sensitive to SAH inhibition, with a Ki of 8 muM. The enzyme responsible for forming m2-guanine between the dihydrouridine and anticodon loops (m2-guanine methyltransferase II) has a Ki of 0.3 muM, while m1-adenine methyltransferase shows intermediate sensitivity to SAH (Ki = 2.4 muM). All three methyltransferases have similar Km's for the S-adenosylmethionine substrate (1.5-2.0 muM). These results are consistent with the hypothesis that activity of individual tRNA methyltransferases may be controlled by enzyme systems which alter cellular SAH levels. | lld:pubmed |
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| pubmed-article:1208211 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1208211 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1208211 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1208211 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1208211 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1208211 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:1208211 | pubmed:author | pubmed-author:LeboyP SPS | lld:pubmed |
| pubmed-article:1208211 | pubmed:author | pubmed-author:GlickJ MJM | lld:pubmed |
| pubmed-article:1208211 | pubmed:author | pubmed-author:RoseAA | lld:pubmed |
| pubmed-article:1208211 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1208211 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:1208211 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1208211 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1208211 | pubmed:pagination | 1639-51 | lld:pubmed |
| pubmed-article:1208211 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1208211 | pubmed:meshHeading | pubmed-meshheading:1208211-... | lld:pubmed |
| pubmed-article:1208211 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:1208211 | pubmed:articleTitle | S-adenosylhomocysteine inhibition of three purified tRNA methyltransferases from rat liver. | lld:pubmed |
| pubmed-article:1208211 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1208211 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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