2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase (BphD)

2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, commonly known as BphD, is a bacterial enzyme that plays a critical role in the aerobic degradation of biphenyl and polychlorinated biphenyls (PCBs) (UniProt: P47230). It belongs to the alpha/beta hydrolase fold superfamily and specifically catalyzes the hydrolytic cleavage of a carbon-carbon bond in 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate (HOPDA) to produce benzoate and 2-hydroxypenta-2,4-dienoate (PubMed: 10411744). This reaction is a key step in the meta-cleavage pathway of aromatic compounds, allowing bacteria to utilize biphenyl as a carbon and energy source (BRENDA: EC 3.7.1.8). While not a therapeutic target for human diseases, BphD is of significant interest in environmental biotechnology and bioremediation due to the persistence and toxicity of PCBs in the environment. Research on BphD often focuses on its substrate specificity and catalytic mechanism to engineer more efficient enzymes for the detoxification of halogenated aromatic pollutants. There are currently no known drugs that target this enzyme for clinical use, as its primary relevance lies in microbial ecology and industrial waste management.

Other names

BphDHOPDA hydrolase2-hydroxy-6-oxo-phenylhexa-2,4-dienoate hydrolase2-hydroxy-6-oxo-6-phenyl-hexa-2,4-dienoate hydrolase

Not applicable as there are no known therapeutic drugs targeting this enzyme.