EC Number   |
Metals/Ions |
Reference |
|---|
    2.5.1.55 | Ba2+ |
1 mM, 5-10% stimulation |
637395 |
| 2.5.1.55 | Ba2+ |
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4 |
709520 |
| 2.5.1.55 | Ca2+ |
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4 |
709520 |
| 2.5.1.55 | Cd2+ |
0.05 mM |
685148 |
| 2.5.1.55 | Cd2+ |
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes |
710528 |
| 2.5.1.55 | Cd2+ |
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252 |
738157 |
| 2.5.1.55 | Cd2+ |
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4 |
709520 |
| 2.5.1.55 | Cd2+ |
destabilizes the enzyme, overview |
737680 |
| 2.5.1.55 | Cd2+ |
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost |
637412 |
| 2.5.1.55 | Cd2+ |
increase in steady-state rate of wild-type enzyme, Km: 0.0006 mM |
659404 |
