Control of catechol meta-cleavage pathway in Alcaligenes eutrophus

J Bacteriol. 1983 Jun;154(3):1363-70. doi: 10.1128/JB.154.3.1363-1370.1983.

Abstract

Alcaligenes eutrophus 335 (ATCC 17697) metabolizes phenol and p-cresol via a catechol meta-cleavage pathway. Studies with mutant strains, each defective in an enzyme of the pathway, showed that the six enzymes assayed are induced by the primary substrate. Studies with a putative polarity mutant defective in the expression of aldehyde dehydrogenase suggested that the structural genes encoding this and subsequent enzymes of the pathway exist in the same operon. From studies with mutant strains that constitutively synthesize catechol 2,3-oxygenase and subsequent enzymes and from the coordination of repression of these enzymes by p-toluate, benzoate, and acetate, it is proposed the catechol 2,3-oxygenase structural gene is situated in this operon (2,3-oxygenase operon). Studies with regulatory mutant strains suggest that the 2,3-oxygenase operon is under negative control.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcaligenes / enzymology*
  • Alcaligenes / genetics
  • Benzoates* / pharmacology
  • Benzoic Acid
  • Catechol 2,3-Dioxygenase
  • Catechols / metabolism*
  • Cresols / metabolism*
  • Dioxygenases*
  • Enzyme Induction
  • Enzyme Repression
  • Gene Expression
  • Genes, Regulator
  • Lactates / metabolism
  • Lactic Acid
  • Mixed Function Oxygenases / metabolism
  • Mutation
  • Operon
  • Oxygenases / genetics
  • Oxygenases / metabolism
  • Phenol
  • Phenols / metabolism*

Substances

  • Benzoates
  • Catechols
  • Cresols
  • Lactates
  • Phenols
  • 4-cresol
  • Phenol
  • Lactic Acid
  • Benzoic Acid
  • 4-toluic acid
  • Mixed Function Oxygenases
  • Oxygenases
  • Dioxygenases
  • Catechol 2,3-Dioxygenase
  • phenol 2-monooxygenase
  • catechol