2'-hydroxybiphenyl-2-sulfinate desulfinase
From Wikipedia, the free encyclopedia
In enzymology, a 2'-hydroxybiphenyl-2-sulfinate desulfinase (EC 3.13.1.3) is an enzyme that catalyzes the chemical reaction
- 2'-hydroxybiphenyl-2-sulfinate + H2O 2-hydroxybiphenyl + sulfite
Thus, the two substrates of this enzyme are 2'-hydroxybiphenyl-2-sulfinate and H2O, whereas its two products are 2-hydroxybiphenyl and sulfite.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-sulfur bonds. The systematic name of this enzyme class is 2'-hydroxybiphenyl-2-sulfinate sulfohydrolase. Other names in common use include gene dszB-encoded hydrolase, 2-(2-hydroxyphenyl) benzenesulfinate:H2O hydrolase, DszB, HBPSi desulfinase, 2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase, HPBS desulfinase, 2-(2-hydroxyphenyl)benzenesulfinate hydrolase, 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase, and 2-(2-hydroxyphenyl)benzenesulfinate desulfinase.
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[edit] Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2DE2, 2DE3, and 2DE4.
[edit] References
- IUBMB entry for 3.13.1.3
- BRENDA references for 3.13.1.3 (Recommended.)
- PubMed references for 3.13.1.3
- PubMed Central references for 3.13.1.3
- Google Scholar references for 3.13.1.3
- Oldfield C, Pogrebinsky O, Simmonds J, Olson ES, Kulpa CF (Pt 9). "Elucidation of the metabolic pathway for dibenzothiophene desulphurization by Rhodococcus sp. strain IGTS8 (ATCC 53968)". Microbiology. 143: 2961–73. PMID 9308179.
- Hirakawa Y, Suzuki M, Maruhashi K, Izumi Y, Kurane R (2002). "A novel enzyme, 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB), from a dibenzothiophene-desulfurizing bacterium Rhodococcus erythropolis KA2-5-1: gene overexpression and enzyme characterization". Biochim. Biophys. Acta. 1598: 122–30. PMID 12147352.
- R, Ruckman E, Cody M, Mrachko GT (2003). "Purification and characterization of the aromatic desulfinase, 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase". Arch. Biochem. Biophys. 415: 14–23. doi: . PMID 12801508.