Char, Shobha and Gopinathan, Karumathil P (1986) Arginyl-tRNA Synthetase from Mycobacterium smegmatis SN2: Purification and Kinetic Mechanism. In: The Journal of Biochemistry, 100 (2). pp. 349-357.
Full text not available from this repository. (Request a copy)Abstract
Arginyl-tRNA synthetase $[L-Arg: tRNA^{Arg})$ ligase (AMP forming) EC 6.1.1.19 [EC]] has been purified to homogeneity from Mycobacterium smegmatis SN2. The enzyme is a monomer of molecular weight 56,000. The kinetic patterns obtained by initial velocity and product inhibition studies are consistent with a rapid equilibrium random ter-ter mechanism. Polyamines stimulated the formation of arginyl-tRNA, the stimulation being more significant at sub-optimal $Mg^{2+}$ concentrations. Initial velocity studies performed in the presence of sub-optimal $Mg^{2+}$ and spermine also indicated that the kinetic mechanism remained sequential random. Various attempts to reveal the formation of enzyme-bound arginyl-adenylate provided no evidence for its existence. The reverse reaction, i.e the deacylation of arginyl-tRNA, required both AMP and $PP_1$. This observation is consistent with the mechanism proposed.
| Item Type: | Journal Article |
|---|---|
| Publication: | The Journal of Biochemistry |
| Publisher: | Japanese Biochemical Society |
| Additional Information: | Copyright of this article belongs to Japanese Biochemical Society. |
| Department/Centre: | Division of Biological Sciences > Microbiology & Cell Biology |
| Date Deposited: | 15 Jul 2008 |
| Last Modified: | 27 Aug 2008 13:31 |
| URI: | http://eprints.iisc.ac.in/id/eprint/14680 |
Actions (login required)
 |
View Item |
