EC Number |
Metals/Ions |
Reference |
---|
2.3.1.169 | CO |
a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate |
644678, 644854, 644857 |
2.3.1.169 | CO |
cobalt is the active site for the methyltransfer reaction |
644864 |
2.3.1.169 | Co3+ |
part of the methylcorrinoid protein |
720372 |
2.3.1.169 | copper |
or iron, required. Copper is one of the most abundant metal species within the cells |
736020 |
2.3.1.169 | 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 |
660349 |
2.3.1.169 | Cu |
the Ni in cluster A can be replaced by Cu yielding an inactive form of the acetyl-CoA synthase |
660370 |
2.3.1.169 | Cu+ |
capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex |
658436 |
2.3.1.169 | Cu2+ |
the enzyme has a metallocofactor containing iron, sulfur, copper, and nickel, the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site |
644679 |
2.3.1.169 | Fe |
a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis |
644858 |
2.3.1.169 | Fe |
corrinoid/iron-sulfur protein required |
390465, 390474, 390475, 644674, 644678, 644850, 644851, 644854, 644855, 644857, 644858, 644861, 644862, 644863 |