4-hydroxybenzoyl-CoA thioesterase (4-HBA-CoA thioesterase)

4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) is a bacterial enzyme that plays a critical role in the aerobic degradation of halogenated aromatic compounds, specifically within the 4-chlorobenzoate (4-CBA) dehalogenation pathway [PubMed: 9605334]. It specifically catalyzes the final step of this pathway by hydrolyzing 4-hydroxybenzoyl-CoA into 4-hydroxybenzoate and free coenzyme A [UniProt: P56851]. The enzyme is a member of the HotDog fold superfamily, characterized by a structural motif where an antiparallel beta-sheet wraps around a central hydrophobic alpha-helix [PubMed: 12484756]. While essential for the metabolic versatility of soil bacteria like Arthrobacter and Pseudomonas, it is not considered a therapeutic target for human disease and has no known human homologs [BRENDA: EC 3.1.2.23]. Its primary significance lies in the field of environmental biotechnology and bioremediation for the detoxification of chlorinated pollutants. The catalytic mechanism involves a conserved glutamate residue that activates a water molecule for nucleophilic attack on the thioester carbonyl [PubMed: 11861913]. There are currently no drugs developed to target this enzyme, and it is not associated with any human clinical conditions.

Other names

4-hydroxybenzoyl-CoA hydrolase4-hydroxybenzoyl-coenzyme A thioesterasefcbC4-hydroxybenzoate-CoA thioesterase

No therapeutic drugs are currently known to target this enzyme. Its endogenous catalytic mechanism involves the hydrolysis of the thioester bond in 4-hydroxybenzoyl-CoA via a water molecule activated by a catalytic glutamate residue [PubMed: 9605334].