Catechol oxygenase induction in Pseudomonas aeruginosa |
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Authors: | D. R. Farr and R. B. Cain |
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Affiliation: | Microbiology Group, Department of Botany, University of Newcastle upon Tyne |
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Abstract: | 1. The transfer from benzenesulphonate to benzoate as a growth substrate for Pseudomonas aeruginosa strain A resulted in a change in the enzymic route by which catechol was degraded; at intermediate stages it was possible to obtain cells containing the enzymes of both the ;ortho' and ;meta' metabolic pathways. 2. A similar result was effected by the reverse transfer, benzoate to benzenesulphonate. 3. Catechol itself always elicited a catechol 2,3-oxygenase in uninduced cells, but the product of this reaction, 2-hydroxymuconic semialdehyde, and biochemically related compounds such as 4-hydroxy-2-oxovalerate, unexpectedly induced a catechol 1,2-oxygenase. 4. Both types of catechol oxygenase are strongly repressed by the metabolic end products of both the ;ortho' and ;meta' pathways, but there was no inhibition of enzymic activity by these end products. |
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