Structural Insights into Dihydroxylation of Terephthalate, a Product of Polyethylene Terephthalate Degradation.

ABSTRACT: Biodegradation of terephthalate (TPA) is a highly desired catabolic process for the bacterial utilization of this polyethylene terephthalate (PET) depolymerization product, but to date, the structure of terephthalate dioxygenase (TPDO), a Rieske oxygenase (RO) that catalyzes the dihydroxylation of TPA to a cis-diol, is unavailable. In this study, we characterized the steady-state kinetics and first crystal structure of TPDO from Comamonas testosteroni KF1 (TPDO_KF1). TPDO_KF1 exhibited substrate specificity for TPA (k_cat/K_m = 57 ± 9 mM^-1 s^-1). The TPDO_KF1 structure harbors characteristic RO features as well as a unique catalytic domain that rationalizes the enzyme's function. The docking and mut

SUBMITTER: Mahto JK 

PROVIDER: S-EPMC8923216 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature