EC Number |
Metals/Ions |
Reference |
---|
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 | Cd2+ |
highly activates by 4fold |
762233 |
2.7.1.180 | Co2+ |
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 | Mg2+ |
required |
761498 |
2.7.1.180 | Mg2+ |
required for catalysis, Mg2+ does not play a major role in stabilizing the interaction of the protein with FAD, Mg2+ in the preferred divalent cation |
762233 |
2.7.1.180 | Mg2+ |
required, dependent on, Mg2+ ion is directly involved in catalysis. A single metal ion is bound in the wild-type enzyme and mutant Ftp_EcE169K structures. The inhibited mutant Ftp_EcY60N contains a bimetal Mg2+ center |
757628 |
2.7.1.180 | Mn2+ |
activates |
762233 |