PMID:3045758
| Citation |
Goodman, R and Schwartz, I (1988) Kinetic analysis of an E.coli phenylalanine-tRNA synthetase mutant. Nucleic Acids Res. 16:7477-86 |
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| Abstract |
A mutation in the pheS gene, encoding phenylalanyl-tRNA synthetase, in E. coli NP37 confers temperature-sensitivity on the organism. A five-fold increase in tRNA(phe) levels complements the mutation. Analysis of the kinetic properties of the mutant enzyme indicates that the KM is 20-fold higher than the wild-type and the dissociation constant of the tRNA(phe)-synthetase complex for the mutant is at least 10-fold higher. These results indicate that the mutation in E. coli NP37 directly affects the tRNA(phe) binding site on the cognate synthetase. |
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| Keywords |
Amino Acyl-tRNA Synthetases/genetics; Escherichia coli/genetics; Genetic Complementation Test; Kinetics; Mutation; Phenylalanine-tRNA Ligase/genetics; Phenylalanine-tRNA Ligase/metabolism; RNA, Transfer, Amino Acid-Specific/genetics; RNA, Transfer, Phe/genetics; RNA, Transfer, Phe/metabolism; Temperature |
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