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Literature summary for 3.13.1.3 extracted from

  • Geronimo, I.; Nigam, S.R.; Payne, C.M.
    Desulfination by 2-hydroxybiphenyl-2-sulfinate desulfinase proceeds via electrophilic aromatic substitution by the cysteine-27 proton (2017), Chem. Sci., 8, 5078-5086 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2'-hydroxybiphenyl-2-sulfinate + H2O Rhodococcus erythropolis 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 2-hydroxybiphenyl + sulfite
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Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis Q6WE14
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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?
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
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?

Synonyms

Synonyms Comment Organism
DszB
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Rhodococcus erythropolis

General Information

General Information Comment Organism
metabolism 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