Initial steps in the anaerobic degradation of 3,4,5-trihydroxybenzoate by Eubacterium oxidoreducens: Characterization of mutants and role of 1,2,3,5- tetrahydroxybenzene

J. D. Haddock, J. G. Ferry

Research output: Contribution to journalArticle

24 Scopus citations

Abstract

Chemical mutagenesis and antibiotic enrichment techniques were used to isolate five mutant strains of the obligate anaerobe Eubacterium oxidoreducens that were unable to grow on 3,4,5-trihydroxybenzoate (gallate). Two strains could not transform gallate and showed no detectable gallate decarboxylase activity. Two other strains transformed gallate to pyrogallol and dihydrophloroglucinol but lacked the hydrolase activity responsible for ring cleavage. A fifth strain accumulated pyrogallol, although it contained adequate levels of the enzymes proposed for the complete transformation of gallate to the ring cleavage product. The conversion of pyrogallol to phloroglucinol by cell extract of the wild-type strain was dependent on the addition of 1,2,3,5-tetrahydroxybenzene or dimethyl sulfoxide. This activity was induced by growth on gallate, while the other enzymes involved in the initial reactions of gallate catabolism were constitutively expressed during growth on crotonate. The results confirm the initial steps in the pathway previously proposed for the metabolism of gallate by E. oxidoreducens, except for the conversion of pyrogallol to phloroglucinol.

Original languageEnglish (US)
Pages (from-to)669-673
Number of pages5
JournalJournal of bacteriology
Volume175
Issue number3
DOIs
Publication statusPublished - Jan 1 1993

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this