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Archives of Microbiology

, Volume 132, Issue 3, pp 270–275 | Cite as

An Escherichia coli mutant defective in the NAD-dependent succinate semialdehyde dehydrogenase

  • Michael A. Skinner
  • Ronald A. Cooper
Original Papers

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.

Key words

Escherichia coli Succinate semialdehyde dehydrogenase Aromatic catabolism Hydroxyphenylacetate Genetic mapping 

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Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • Michael A. Skinner
    • 1
  • Ronald A. Cooper
    • 1
  1. 1.Department of BiochemistryUniversity of LeicesterLeicesterEngland

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