2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB)

2'-hydroxybiphenyl-2-sulfinate desulfinase, commonly known as DszB, is a microbial enzyme that catalyzes the final and rate-limiting step of the 4S biodesulfurization pathway. This pathway is utilized by bacteria such as Rhodococcus erythropolis to remove sulfur from aromatic heterocyclic compounds like dibenzothiophene (DBT) without degrading the carbon skeleton (Oldfield et al., 1997, PubMed: 9290208). The enzyme specifically facilitates the hydrolysis of 2'-hydroxybiphenyl-2-sulfinate (HBPS) to produce 2-hydroxybiphenyl (HBP) and sulfite (Lee et al., 2003, PubMed: 12624197). Structurally, DszB is a member of the nitrilase superfamily and employs a conserved Cys-Glu-Lys catalytic triad to execute the cleavage of the carbon-sulfur bond (UniProt: P54997). Because it is not found in human physiology and does not participate in human disease, it is not considered a therapeutic target for drug development. Instead, its primary significance lies in environmental biotechnology and the petrochemical industry, where it is studied for the production of cleaner-burning, low-sulfur fossil fuels (Bone et al., 2006, PubMed: 16451306).

Other names

DszBHBPS desulfinase2-(2-hydroxyphenyl)benzenesulfinate desulfinase2'-hydroxybiphenyl-2-sulfinate sulfohydrolase

Not applicable as this is a microbial enzyme used in industrial biocatalysis rather than a therapeutic target.