摘要
Escherichia coli leucyl-tRNA synthetase (LeuRS) is one of aminoacyl-tRNA synthetases (aaRSs) and belongs to class 1 aaRSs. The apparent steady-state kinetics of the aminoacylation reaction catalyzed by LeuRS in the presence of some RE3+ were studied. The results show that Mg2+ can be substituted by RE3+ for the aminoacylation reaction. The apparent K-m values for ATP and leucine are markedly different between native and Mg2+-free tRNA(1)(Leu). At high concentration of ATP there is inhibitory effect on Mg2+-free tRNA but not on native tRNA, which indicates that metal ions are a substrate of the aminoacylation reaction.
Escherichia coli leucyl-tRNA synthetase (LeuRS) is one of aminoacyl-tRNA synthetases (aaRSs) and belongs to class 1 aaRSs. The apparent steady-state kinetics of the aminoacylation reaction catalyzed by LeuRS in the presence of some RE3+ were studied. The results show that Mg2+ can be substituted by RE3+ for the aminoacylation reaction. The apparent K-m values for ATP and leucine are markedly different between native and Mg2+-free tRNA(1)(Leu). At high concentration of ATP there is inhibitory effect on Mg2+-free tRNA but not on native tRNA, which indicates that metal ions are a substrate of the aminoacylation reaction.
基金
ProjectsupportbythePh .D .ProgramFoundationoftheStateEducationCommissionofChina (970 0 1 0 4 )
thePh .D .Foun dationofHebeiP
