1887

Abstract

SUMMARY

The homoserine--transsuccinylase activity of three kinds of methionine- excreting mutants of was examined. In a mutant the enzyme was resistant to inhibition by methionine or its analogue α-methyl-methionine. Feedback inhibition in a and a strain was normal. was dominant to only when coupled in the position with the wild-type allele of the closely-linked (homoserine--transsuccinylase) gene, and a deletion analysis of nine mutations showed that they were all located within the gene. Thus both the regulatory and catalytic sites of homoserine--transsuccinylase are specified by a single polypeptide species. An estimate was made of the length of the gene, based on recombination data.

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1970-09-01
2024-04-25
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