Deobagkar, Dilip N and Gopinathan, KP (1976) Two forms of methionyl-transfer RNA synthetase from Mycobacterium Smegmatis. In: Biochemical and Biophysical Research Communications, 71 (4). pp. 939-951.
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Two methionyl-transfer RNA synthetases (A and B forms) have been isolated from Image . The homogeneous preparations of the enzymes showed 1500 fold increase in specific activity in aminoacylation of methionine specific tRNA. The A and B forms differed in their specificity of aminoacylation of tRNAmMet and tRNAfMet; enzyme B exhibited much higher specificity for tRNAfMet. The molecular activities of A and B enzymes for aminoacid and tRNA were identical. The turnover number for aminoacid was 27 fold greater than that for tRNA, while the Km values for tRNA were lower by a factor of 106 as compared to the aminoacid. Both the enzymes catalysed ATP-pyrophosphate exchange reaction to the same extent.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elservier sciecne|
|Department/Centre:||Division of Biological Sciences > Microbiology & Cell Biology|
|Date Deposited:||09 Dec 2009 12:02|
|Last Modified:||19 Sep 2010 05:49|
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