The Enzyme Database

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Accepted name: dibenzothiophene monooxygenase
Reaction: dibenzothiophene + 2 FMNH2 + 2 O2 = dibenzothiophene-5,5-dioxide + 2 FMN + 2 H2O (overall reaction)
(1a) dibenzothiophene + FMNH2 + O2 = dibenzothiophene-5-oxide + FMN + H2O
(1b) dibenzothiophene-5-oxide + FMNH2 + O2 = dibenzothiophene-5,5-dioxide + FMN + H2O
Glossary: dibenzothiophene-5,5-dioxide = dibenzothiophene sulfone
Other name(s): dszC (gene name)
Systematic name: dibenzothiophene,FMNH2:oxygen oxidoreductase
Comments: This bacterial enzyme catalyses the first two steps in the desulfurization pathway of dibenzothiophenes, the oxidation of dibenzothiophene into dibenzothiophene sulfone via dibenzothiophene-5-oxide. The enzyme forms a two-component system with a dedicated NADH-dependent FMN reductase (EC encoded by the dszD gene, which also interacts with EC, dibenzothiophene sulfone monooxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Gray, K.A., Pogrebinsky, O.S., Mrachko, G.T., Xi, L., Monticello, D.J. and Squires, C.H. Molecular mechanisms of biocatalytic desulfurization of fossil fuels. Nat. Biotechnol. 14 (1996) 1705–1709. [DOI] [PMID: 9634856]
2.  Liu, S., Zhang, C., Su, T., Wei, T., Zhu, D., Wang, K., Huang, Y., Dong, Y., Yin, K., Xu, S., Xu, P. and Gu, L. Crystal structure of DszC from Rhodococcus sp. XP at 1.79 Å. Proteins 82 (2014) 1708–1720. [DOI] [PMID: 24470304]
3.  Guan, L.J., Lee, W.C., Wang, S., Ohshiro, T., Izumi, Y., Ohtsuka, J. and Tanokura, M. Crystal structures of apo-DszC and FMN-bound DszC from Rhodococcus erythropolis D-1. FEBS J. 282 (2015) 3126–3135. [DOI] [PMID: 25627402]
[EC created 2016]

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