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. 1968 May;95(5):1672–1679. doi: 10.1128/jb.95.5.1672-1679.1968

Isoleucine and Valine Metabolism of Escherichia coli XV. Biochemical Properties of Mutants Resistant to Thiaisoleucine

A Szentirmai a,1, M Szentirmai a,1, H E Umbarger a
PMCID: PMC252194  PMID: 4297021

Abstract

Thiaisoleucine-resistant mutants of Escherichia coli strain K-12 which exhibited reduced isoleucyl soluble ribonucleic acid synthetase activity were isolated. Resistance was apparently achieved by the selection of a synthetase with a 10-fold decrease in apparent affinity for thiaisoleucine. This mutation also resulted in a 2.5-fold decrease in apparent affinity for the natural substrate, l-isoleucine, and less activity than found in wild type. The mutants grew more slowly than wild type and were derepressed for three of the five enzymes in the pathways to isoleucine and valine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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