Char, S. ; Gopinathan, K. P. (1985) Purification and kinetic mechanism of lysyl-tRNA synthetase from Mycobacterium smegmatis SN2 Biochemistry International, 11 (6). pp. 893-902. ISSN 0158-5231
Full text not available from this repository.
Abstract
Lysyl-tRNA synthetase [L-lys:tRNAlys ligase (AMP forming) EC:6.1.1.6] has been purified to homogeneity from Mycobacterium smegmatis SN2. The enzyme is a dimer of molecular weight 126,000 and is composed of identical subunits. A detailed analysis of the kinetic mechanism of the lysyl-tRNA synthetase has been carried out. A rapid equilibrium random ter ter mechanism is proposed based on initial velocity and product inhibition studies. There is no evidence for the formation of enzyme-bound lysyl-adenylate. The reverse reaction, studied by the deacylation of lysyl-tRNA, requires the presence of both AMP and PPi. This observation is consistent with the mechanism proposed.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to International Union of Biochemistry. |
| ID Code: | 88090 |
| Deposited On: | 27 Mar 2012 08:17 |
| Last Modified: | 27 Mar 2012 08:17 |
Repository Staff Only: item control page
