EC	1.14.14.21
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 1.5.1.42) encoded by the dszD gene, which also interacts with EC 1.14.14.22, dibenzothiophene sulfone monooxygenase.
References:	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. [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. [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. [PMID: 25627402]
[EC 1.14.14.21 created 2016]