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Kinetic analysis of an E.coli phenylalanine-tRNA synthetase mutant.
Authors:R Goodman and I Schwartz
Affiliation:Department of Biochemistry, New York Medical College, Valhalla 10595.
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.
Keywords:
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