EC Number   |
Metals/Ions |
Reference |
|---|
    6.2.1.1 | Co2+ |
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding |
563 |
| 6.2.1.1 | Cu2+ |
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding |
563 |
| 6.2.1.1 | Fe2+ |
CODH/ACS uses a Ni-Fe-S center called the C-cluster to reduce carbon dioxide to carbon monoxide and uses a second Ni-Fe-S center, called the A-cluster, to assemble acetyl-CoA from a methyl group, coenzyme A, and C-cluster-generated CO |
685228 |
| 6.2.1.1 | Fe2+ |
the A-cluster of acetyl-coenzyme A synthase consists of an [Fe4S4] cubane bridged to a [NipNid] centre via C509 cysteinate. The bridging cysteinate, which can be substituted by histidine imidazole, mediates communication between the [Fe4S4] cubane and the [NipNid] centre during the synthesis of acetyl-CoA |
714724 |
| 6.2.1.1 | Fe2+ |
the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, bifunctional Ni-Fe-S containing ACS/CODH |
687824 |
| 6.2.1.1 | Fe2+ |
the enzyme contains a ([Fe4S4]2+ Nip2+ Nid2+) cluster in the alpha-subunit, exchange coupling pathway between the Sc = 1/2 [Fe4S4]1+ cluster and the SNi = 1/2 Nip 1+ involves the cysteinate that links one cluster site, previously labeled FeD, to the Ni1+, structure and spectral analysis, overview |
692769 |
| 6.2.1.1 | Fe2+ |
two types of divalent metal ion requirement, 1. Mg2+, Mn2+, Fe2+, Co2+ or Ca2+ required for the formation of the enzyme-bound acetyl adenylate, 2. Ni2+, Cd2+, Fe2+ or Cu2+ required for adenylate binding |
563 |
| 6.2.1.1 | K+ |
absolute requirement for a monovalent cation, stimulates, Km: 14.3 mM, inhibition above 0.1 M |
560 |
| 6.2.1.1 | K+ |
activates, absolute requirement for certain monovalent cations, no inhibition at high concentrations |
563 |
| 6.2.1.1 | K+ |
KCl increases the activity of the enzyme about 60% at 5 mM and 80% at 20 mM |
568 |
