Related Experiment Videos
Protocatechuate is not metabolized via catechol in Enterobacter aerogenes
1Department of Biology, Yale University, New Haven, Connecticut 06511.
Journal of Bacteriology
|December 1, 1987
Summary
Enterobacter aerogenes primarily metabolizes protocatechuate via oxygenative cleavage, not nonoxidative decarboxylation to catechol. Mutant analysis confirmed the oxygenative pathway
Area of Science:
- Microbial metabolism
- Bacterial biochemistry
- Enzyme kinetics
Background:
- Protocatechuate is a common aromatic compound metabolized by bacteria.
- Typically, bacterial protocatechuate metabolism involves oxygenative cleavage to beta-carboxymuconate.
- A proposed alternative pathway in Enterobacter aerogenes involves nonoxidative decarboxylation to catechol.
Purpose of the Study:
- To investigate the metabolic pathway of protocatechuate in Enterobacter aerogenes.
- To determine the significance of the proposed nonoxidative decarboxylation pathway versus the canonical oxygenative cleavage pathway.
Main Methods:
- Construction and analysis of mutant strains of E. aerogenes.
- Assessing protocatechuate utilization in wild-type and mutant strains.
- Monitoring enzyme induction related to protocatechuate and catechol metabolism.
Main Results:
- Mutations affecting catechol metabolism did not impede protocatechuate utilization, indicating the nonoxidative pathway is not significant.
- Enzymes for oxygenative cleavage and further metabolism of protocatechuate were induced during its metabolism.
- Inactivation of the oxygenative pathway genes prevented protocatechuate degradation.
- E. aerogenes exhibited broad inductive control over genes for protocatechuate and catechol metabolism, suggesting multiple metabolite triggers.
Conclusions:
- The primary route for protocatechuate metabolism in E. aerogenes is oxygenative cleavage.
- The proposed nonoxidative decarboxylation pathway plays a minor role, if any.
- Gene expression for protocatechuate metabolism is broadly regulated by various metabolites.