The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: 2′-hydroxybiphenyl-2-sulfinate desulfinase
Reaction: 2′-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
For diagram of reaction, click here
Other name(s): 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; 2-(2-hydroxyphenyl)benzenesulfinate desulfinase
Systematic name: 2′-hydroxybiphenyl-2-sulfinate sulfohydrolase
Comments: The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date [2].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 198154-06-2
1.  Oldfield, C., Pogrebinsky, O., Simmonds, J., Ölson, E.S. and Kulpa, C.F. Elucidation of the metabolic pathway for dibenzothiophene desulfurization by Rhodococcus sp. strain IGTS8 (ATCC 53968). Microbiology 143 (1997) 2961–2973. [DOI] [PMID: 9308179]
2.  Nakayama, N., Matsubara, T., Ohshiro, T., Moroto, Y., Kawata, Y., Koizumi, K., Hirakawa, Y., Suzuki, M., Maruhashi, K., Izumi, Y. and Kurane, R. 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 (2002) 122–130. [DOI] [PMID: 12147352]
3.  Watkins, L.M., Rodriguez, R., Schneider, D., Broderick, R., Cruz, M., Chambers, R., Ruckman, E., Cody, M. and Mrachko, G.T. Purification and characterization of the aromatic desulfinase, 2-(2′-hydroxyphenyl)benzenesulfinate desulfinase. Arch. Biochem. Biophys. 415 (2003) 14–23. [DOI] [PMID: 12801508]
[EC created 2000 as EC, transferred 2005 to EC]

Data © 2001–2023 IUBMB
Web site © 2005–2023 Andrew McDonald