Structural characterization of thiolase and decarboxylase enzymes for biotechnological application in microbial degradation of water pollutants

The central theme of this thesis is to understand the microbial degradation of aromatic compounds. Two enzymes are selected for study, which belong to the central β-ketoadipate pathway, a key aromatic degradation pathway found in Pseudomonas Sp., Acinetobacter Sp. The first protein, β-keto acyl CoA thiolase (PcaF), catalyzes the last step of the β-ketoadipate pathway and the second protein of interest, γ-caboxymuconolactone decarboxylase (PcaC), belong to the protocatechuate branch of the β-ketoadipate pathway. These two proteins are located at two crucial point in the pathway, thus understanding these two catabolic enzymes will aid in development of better bioremediation designs.