3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	-	Rhodococcus erythropolis	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	highly specific for	Rhodococcus erythropolis	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	the enzyme is involved in biodesulfurization, an option for enzymatically removing sulfur from the recalcitrant thiophenic derivatives that comprise the majority of organosulfur compounds remaining in hydrotreated petroleum products	Rhodococcus erythropolis	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	electrophilic aromatic substitution mechanism. The catalytic cysteine in the enzyme DszB (C27) acts as a proton donor. The nascent ionized C27 at the transition state is stabilized by H60, whose charge is modulated by hydrogen bond interaction with S25	Rhodococcus erythropolis	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	-	Rhodococcus erythropolis IGTS8 / ATCC 53968	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	-	Rhodococcus erythropolis IGTS8	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	-	Rhodococcus erythropolis KA2-5-1	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2'-hydroxybiphenyl-2-sulfinate + H2O	highly specific for	Rhodococcus erythropolis KA2-5-1	2-hydroxybiphenyl + sulfite	-	?	364463	
3.13.1.3	2-(2'-hydroxyphenyl)benzenesulfinate + H2O	-	Rhodococcus rhodochrous	2-hydroxybiphenyl + sulfite	-	?	139732	
3.13.1.3	2-(2'-hydroxyphenyl)benzenesulfinate + H2O	-	Paenibacillus sp.	2-hydroxybiphenyl + sulfite	-	ir	139732