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Literature summary for 2.3.1.169 extracted from

  • Seravalli, J.; Gu, W.; Tam, A.; Strauss, E.; Begley, T.P.; Cramer, S.P.; Ragsdale, S.W.
    Functional copper at the acetyl-CoA synthase active site (2003), Proc. Natl. Acad. Sci. USA, 100, 3689-3694.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
copper the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure. Cu-SCoA intermediate in the mechanism of acetyl-CoA synthesis. Essential and functional role for copper in the enzyme Moorella thermoacetica
Iron the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site Moorella thermoacetica
Nickel the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure Moorella thermoacetica

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
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