An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase |
| |
Authors: | Michael A. Skinner Ronald A. Cooper |
| |
Affiliation: | (1) Department of Biochemistry, University of Leicester, LE1 7RH Leicester, England;(2) Institut für Virologie, Universität Würzburg, Versbacher Straße 7, D-8700 Würzburg, Federal Republic of Germany |
| |
Abstract: | Escherichia coli mutants, unable to grown on 4-hydroxyphenylacetate, have been isolated and found to be defective in the NAD-dependent succinate semialdehyde dehydrogenase. When the mutants are grown with 4-aminobutyrate as sole nitrogen source an NAD-dependent succinate semialdehyde dehydrogenase seen in the parental strain is absent but, as in the parental strain, an NADP-dependent enzyme is induced. Growth of the mutants is inhibited by 4-hydroxyphenylacetate due to the accumulation of succinate semialdehyde. The mutants are more sensitive to inhibition by exogenous succinate semialdehyde than is the parental strain. Secondary mutants able to grow in the presence of 4-hydroxyphenylacetate but still unable to use it as sole carbon source were defective in early steps of 4-hydroxyphenylacetate catabolism and so did not form succinate semialdehyde from 4-hydroxyphenylacetate. The gene encoding the NAD-dependent succinate semialdehyde dehydrogenase of Escherichia coli K-12 was located at min 34.1 on the genetic map. |
| |
Keywords: | Escherichia coli Succinate semialdehyde dehydrogenase Aromatic catabolism Hydroxyphenylacetate Genetic mapping |
本文献已被 SpringerLink 等数据库收录! |
|