EC 1.14.14.22 - Dibenzothiophene sulfone monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.14.22

Names

Accepted name:
dibenzothiophene sulfone monooxygenase
Other name:
dszA (gene name)
Systematic name:
dibenzothiophene-5,5-dioxide,FMNH2:oxygen oxidoreductase

Reaction

Comments:

This bacterial enzyme catalyses a step in the desulfurization pathway of dibenzothiophenes. 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 1.14.14.21, dibenzothiophene monooxygenase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Gray, K. A., Pogrebinsky, O. S., Mrachko, G. T., Xi, L., Monticello, D. J., Squires, C. H.
    Molecular mechanisms of biocatalytic desulfurization of fossil fuels.
    Nat. Biotechnol. 14: 1705-1709 (1996). [PMID: 9634856]
  2. Ohshiro, T., Kojima, T., Torii, K., Kawasoe, H., Izumi, Y.
    Purification and characterization of dibenzothiophene (DBT) sulfone monooxygenase, an enzyme involved in DBT desulfurization, from Rhodococcus erythropolis D-1.
    J. Biosci. Bioeng. 88: 610-616 (1999). [PMID: 16232672]
  3. Konishi, J., Ishii, Y., Onaka, T., Ohta, Y., Suzuki, M., Maruhashi, K.
    Purification and characterization of dibenzothiophene sulfone monooxygenase and FMN-dependent NADH oxidoreductase from the thermophilic bacterium Paenibacillus sp. strain A11-2.
    J. Biosci. Bioeng. 90: 607-613 (2000). [PMID: 16232919]
  4. Ohshiro, T., Ishii, Y., Matsubara, T., Ueda, K., Izumi, Y., Kino, K., Kirimura, K.
    Dibenzothiophene desulfurizing enzymes from moderately thermophilic bacterium Bacillus subtilis WU-S2B: purification, characterization and overexpression.
    J. Biosci. Bioeng. 100: 266-273 (2005). [PMID: 16243275]

[EC 1.14.14.22 created 2016]