EC Number |
Metals/Ions |
Reference |
---|
2.7.1.180 | Co2+ |
activates |
762233 |
2.7.1.180 | Mn2+ |
activates |
762233 |
2.7.1.180 | Mg2+ |
dependent on |
725516 |
2.7.1.180 | Mg2+ |
dependent on, metal-dependent enzyme |
757628 |
2.7.1.180 | Mg2+ |
dependent on, metal-dependent enzyme, bimetal center in the crystal structure of Escherichia coli Ftp |
757628 |
2.7.1.180 | more |
divalent cations are essential for ApbE activity, and their removal by EDTA abolishes the activity. ApbE is also able to use other divalent cations, such as Mn2+ and Co2+, obtaining a similar activity compared to Mg2+. The coordination sphere of ApbE enzymes largely determines the specificity of the enzyme for the divalent cation |
762233 |
2.7.1.180 | Cd2+ |
highly activates by 4fold |
762233 |
2.7.1.180 | more |
identification of a bimetal center in the crystal structure of Escherichia coli Ftp (Ftp_Ec) |
757628 |
2.7.1.180 | Ca2+ |
presence of a Ca2+ ion in metal site 1 in the apo form of mutant Ftp_EcY60N, the Ca2+ ion serves a role in properly positioning substrate and protein residues |
757628 |
2.7.1.180 | Mg2+ |
required |
761498 |