Purification and kinetic mechanism of lysyl-tRNA synthetase from Mycobacterium smegmatis SN2.
Biochem Int
; 11(6): 893-902, 1985 Dec.
Article
em En
| MEDLINE
| ID: mdl-3853966
ABSTRACT
Lysyl-tRNA synthetase [L-lystRNAlys ligase (AMP forming) EC6.1.1.6] 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.
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Base de dados:
MEDLINE
Assunto principal:
Aminoacil-tRNA Sintetases
/
Lisina-tRNA Ligase
/
Mycobacterium
Idioma:
En
Revista:
Biochem Int
Ano de publicação:
1985
Tipo de documento:
Article