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. 1988 Aug 11;16(15):7477-86.
doi: 10.1093/nar/16.15.7477.

Kinetic analysis of an E.coli phenylalanine-tRNA synthetase mutant

R Goodman  1 , I Schwartz
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Free PMC article

Kinetic analysis of an E.coli phenylalanine-tRNA synthetase mutant

R Goodman et al. Nucleic Acids Res. .
Free PMC article

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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