The control of the enzymes degrading histidine and related imidazolyl derivates in Pseudomonas testosteroni

Biochem J. 1973 Mar;132(3):423-33. doi: 10.1042/bj1320423.


1. The induction of the enzymes for the degradation of l-histidine, imidazolylpropionate and imidazolyl-l-lactate in Pseudomonas testosteroni was investigated. 2. The activities of histidine ammonia-lyase, histidine-2-oxoglutarate aminotransferase and urocanase are consistent with these enzymes being subject to co-ordinate control under most growth conditions. However, a further regulatory mechanism may be superimposed for histidase alone under conditions where degradation of histidine must take place for growth to occur. 3. Experiments with a urocanase(-) mutant show that urocanate is an inducer for the enzymes given above and also for N-formiminoglutamate hydrolyase and N-formylglutamate hydrolase. 4. N-Formiminoglutamate hydrolase and N-formylglutamate hydrolase are also induced by their substrates, and it is suggested that these two enzymes may be different gene products from those expressed in the presence of urocanate. 5. Induction of the enzyme system for the oxidation of imidazolylpropionate is dependent on exposure of cells to this compound.

MeSH terms

  • Biological Transport
  • Carbon Isotopes
  • Enzyme Induction
  • Enzyme Repression
  • Formates
  • Glutamates
  • Histidine / metabolism*
  • Histidine Ammonia-Lyase / biosynthesis
  • Hydrolases / biosynthesis
  • Imidazoles / metabolism*
  • Imines
  • Ketoglutaric Acids
  • Kinetics
  • Models, Biological
  • Mutation
  • Oxygen Consumption
  • Propionates / metabolism
  • Pseudomonas / enzymology*
  • Spectrophotometry, Ultraviolet
  • Time Factors
  • Transaminases / biosynthesis
  • Urocanate Hydratase / biosynthesis


  • Carbon Isotopes
  • Formates
  • Glutamates
  • Imidazoles
  • Imines
  • Ketoglutaric Acids
  • Propionates
  • Histidine
  • Transaminases
  • Hydrolases
  • Urocanate Hydratase
  • Histidine Ammonia-Lyase