EC Number   |
Metals/Ions |
Reference |
|---|
    3.5.1.108 | Co2+ |
0.1 mM, significantly enhances activity |
695538 |
| 3.5.1.108 | Co2+ |
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) |
696193 |
| 3.5.1.108 | Fe2+ |
LpxC exhibits 6-8fold higher activity with a single bound Fe2+ as the cofactor compared to Zn2+-LpxC. The catalytic metal ion bound to Fe2+-EcLpxC is five-coordinate. Both metalloenzymes have a bell-shaped dependence on pH with similar pKa values. Ligand affinity of Fe2+-LpxC compared to the Zn2+ enzyme is altered by up to 6fold. In contrast to Zn2+-LpxC, the activity of Fe2+-LpxC is redox-sensitive, and a time-dependent decrease in activity is observed under aerobic conditions |
718865 |
| 3.5.1.108 | Fe2+ |
the metal bound to LpxC purified from Escherichia coli grown in minimal medium is mainly Fe(II). However, the ratio of iron/zinc bound to LpxC varies with the metal content of the medium. Fe(II) is the thermodynamically favored metal cofactor for LpxC under cellular conditions, but the metal cofactor in LpxC can switch between iron and zinc in response to perturbations in available metal ions |
719894 |
| 3.5.1.108 | Mn2+ |
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) |
696193 |
| 3.5.1.108 | more |
metal-dependent enzyme |
734239 |
| 3.5.1.108 | more |
metalloenzyme |
695628, 698550 |
| 3.5.1.108 | Ni2+ |
incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) |
696193 |
| 3.5.1.108 | Zn2+ |
a mechanism is suggested that includes a transition state pentacoordinate system while the zinc is tetracoordinated in the absence of substrate |
755346 |
| 3.5.1.108 | Zn2+ |
catalytic Zn2+ |
734239 |
