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Nucleic Acids Research, 1975, Vol. 2, No. 10 1639-1652
© 1975

Articles

S-Adenosylhomocysteine inhibition of three purified tRNA methyltransferases from rat liver

Jane M. Glick, Susan Ross and Phoebe S. Leboy

Department of Biochemistry, School of Dental Medicine, University of Pennsylvania Philadelphia, PA 19174, USA

Received May 28, 1975. 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 B uM. The enzyme responsible for forming m2guanine between the dihydrouridine and anticodon loops (m2-guanine methyltransferase II) has a Ki of 0.3 uM, while m1-adenine methyltransferase shows intermediate sensitivity to SAH (Ki = 2.4 µM). All three methyltransferases have similar Km's for the S-adenosylmethionine substrate (1.5–2.0 µM). 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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