EC Number |
Metals/Ions |
Reference |
---|
1.14.14.10 | Mg2+ |
the enzyme shows little preference for Mg-nitrilotriacetate over Co-nitrilotriacetate, Ni-nitrilotriacetate, and Zn-nitrilotriacetate |
717545 |
1.14.14.10 | Mn2+ |
Mn2+ ions are able to replace Mg2+ but lead to a higher uncoupled NADH oxidation and enzyme activity is reduced to 70% of that with MgCl2 |
715329 |
1.14.14.10 | more |
no nitrilotriacetate consumption is observed with Ca2+,Fe2+, Fe3+, Zn2+, Cu2+, or Ni2+ |
715329 |
1.14.14.10 | more |
the enzyme contains less than 0.15 atom of Fe per mol of protein, indicating that neither Fe-sulfur clusters nor cytochromes are present |
715329 |
1.14.14.10 | Ni2+ |
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+ |
717545 |
1.14.14.10 | Zn2+ |
nitrilotriacetate is only a substrate when complexed with cations such as Mg2+, Al3+, Cu2+, Ni2+, Zn2+, Fe2+ or Co2+ |
717545 |