Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1
Autor: | Ronald A. Cooper, David C. N. Jones |
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Rok vydání: | 1990 |
Předmět: |
cis-trans-Isomerases
Gentisates Mutant Biology Biochemistry Microbiology Mixed Function Oxygenases Transduction Genetic Dioxygenase Hydroxybenzoates Genetics Maleylpyruvate isomerase Isomerases Molecular Biology chemistry.chemical_classification Catabolism General Medicine Monooxygenase Chromatography Ion Exchange Klebsiella pneumoniae Enzyme chemistry Hydroxybenzoate Cis-trans-Isomerases Mutation Oxidation-Reduction |
Zdroj: | Archives of Microbiology. 154:489-495 |
ISSN: | 1432-072X 0302-8933 |
Popis: | Growth of Klebsiella pneumoniae M5a1 on 3-hydroxybenzoate leads to the induction of 3-hydroxybenzoate monooxygenase, 2,5-dihydroxybenzoate dioxygenase, maleylpyruvate isomerase and fumaryl-pyruvate hydrolase. Growth in the presence of 2,5-dihydroxybenzoate also induces all of these enzymes including the 3-hydroxybenzoate monooxygenase which is not required for 2,5-dihydroxybenzoate catabolism. Mutants defective in 3-hydroxybenzoate monooxygenase fail to grow on 3-hydroxybenzoate but grow normally on 2,5-dihydroxybenzoate. Mutants lacking maleylpyruvate isomerase fail to grow on 3-hydroxybenzoate and 2,5-dihydroxybenzoate. Both kinds of mutants grow normally on 3,4-dihydroxybenzoate. Mutants defective in maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited. Secondary mutants that have additionally lost 3-hydroxybenzoate monooxygenase are no longer inhibited by the presence of 3-hydroxybenzoate. The 3-hydroxybenzoate monooxygenase gene (mhbM) and the maleylpyruvate isomerase gene (mhbI) are 100% co-transducible by P1 phage. |
Databáze: | OpenAIRE |
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