EC Number   |
Metals/Ions |
Reference |
|---|
   3.5.1.103 | Zn2+ |
a zinc-dependent enzyme, binding structure of the catalytic zinc, overview |
732997 |
| 3.5.1.103 | Co2+ |
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+ |
719933 |
| 3.5.1.103 | Fe2+ |
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+ |
719933 |
| 3.5.1.103 | Mn2+ |
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+ |
719933 |
| 3.5.1.103 | Ni2+ |
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+ |
719933 |
| 3.5.1.103 | Zn2+ |
activity follows the trend Fe2+>Co2+>Zn2+>Mn2+ and Ni2+ |
719933 |
| 3.5.1.103 | Zn2+ |
contains an active site divalent transition metal. MshB activity lost by incubation of the Ni enzyme with 1,10-phenanthroline can be restored following removal of 1,10-phenanthroline by incubation with 0.1 mM Zn2+, Ni2+, Mn2+, or Co2+, the latter promoting the highest activity. Ca2+ and Mg2+ produce no restoration of activity |
701051 |
| 3.5.1.103 | more |
enzyme has a strong preference for the Fe2+ cofactor under anaerobic conditions, regardless of the metal ion content of the medium. The preferred cofactor changes between Zn2+ and Fe2+ depending on the metal ion content of the medium when MshB is purified under aerobic conditions |
719933 |
| 3.5.1.103 | Zn2+ |
metal-dependent enzyme |
752756 |
| 3.5.1.103 | Zn2+ |
metalloprotein, the deacetylase activity is completely dependent on the presence of a divalent metal cation. The Zn2+ is 5 coordinate with 3 residues from MshB (His-13, Asp-16, His-147) and two water molecules |
698727 |
