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Literature summary for 2.8.1.8 extracted from

  • Douglas, P.; Kriek, M.; Bryant, P.; Roach, P.L.
    Lipoyl synthase inserts sulfur atoms into an octanoyl substrate in a stepwise manner (2006), Angew. Chem., 45, 5197-5199.
    View publication on PubMed
Search for more literature for 2.8.1.8

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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Reaction

Reaction Comment Organism Reaction ID
[protein]-N6-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ = [protein]-N6-[(R)-dihydrolipoyl]-L-lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin mechanism: sulfur is first inserted at C6 of octanoyl substrate to form an enzyme bound intermediate. In a subsequent rate determining step, the second sulfur atom is inserted at C8, suggesting an energy profile of the reaction reflecting the relative bond strengths of the primary and secondary C-H bonds to be cleaved at C8 and C6, resp. Saccharolobus solfataricus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information insertion of sulfur into octanoyl groups is first at C6 to form an enzyme bound intermediate, and in a subsequent step a second sulfur is inserted at C8 Saccharolobus solfataricus ?
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