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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1976-3-30
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-10793703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-10793704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-163688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4208689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4261254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4261286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4272661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4325338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4338482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4376890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4553230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4569776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4583670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4596141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4604768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4692843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4919960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-4985261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1208211-5543941
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1639-51
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1208211-Adenine,
pubmed-meshheading:1208211-Animals,
pubmed-meshheading:1208211-Guanine,
pubmed-meshheading:1208211-Homocysteine,
pubmed-meshheading:1208211-Isoenzymes,
pubmed-meshheading:1208211-Kinetics,
pubmed-meshheading:1208211-Liver,
pubmed-meshheading:1208211-Male,
pubmed-meshheading:1208211-Rats,
pubmed-meshheading:1208211-S-Adenosylhomocysteine,
pubmed-meshheading:1208211-Structure-Activity Relationship,
pubmed-meshheading:1208211-tRNA Methyltransferases
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pubmed:year |
1975
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pubmed:articleTitle |
S-adenosylhomocysteine inhibition of three purified tRNA methyltransferases from rat liver.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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