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The metabolic divergence in the meta cleavage of catechols by Pseudomonas putida NCIB 10015. Physiological significance and evolutionary implications.

1 
A reinvestigation of the catabolic pathway(s) used by Pseudomonas putida NCIB 10015 (Dagley's strain) for the degradation of phenol and the cresols has proved the existence of a metabolic divergence after meta cleavage of the catechols formed by hydroxylation of the primary substrates. The ring-fission products of catechol and 4-methylcatechol are shown to be simultaneously catabolized by two different enzymic activities, an NAD+-dependent dehydrogenase and a cofactor-independent hydrolase. The metabolizing activities of both ring-fission products in extracts of cells grown on phenol and the cresols (o-, m- and p-cresol) were found to be non specific; thermal inactivation of extracts of phenol-grown cells has shown that this nonspecificity is attributable to only one enzyme expressing each activity and that the two activities are located on separate proteins. 
 
2 
Extracts of cells grown on all four substrates contain high induced levels of the meta cleavage suite of enzymes functional in the dissimilation of catechol, including both the 4-oxalocrotonate branch (NAD+-dependent 2-hydroxymuconic semialdehyde dehydrogenase, 4-oxalocrotonate tautomerase and 4-oxalocrotonate decarboxylase) and the hydrolytic branch (2-hydroxymuconic semialdehyde hydrolase). 
 
3 
The hydroxylase, oxygenase, dehydrogenase and hydrolase activities are shown to be nonspecific and can also act upon the methyl derivatives of their respective substrates. A constant pattern of specificity was found for these enzymes, independent of the monophenolic substrate used for growth. 
 
4 
From studies with a mutant lacking phenol hydroxylase, the entire suite of meta cleavage enzymes are shown to be coincidently induced from the top by the primary substrate (phenol or the cresols). 
 
5 
The evolutionary and physiological implications of the divergent pathway are discussed.