EC Number   |
Metals/Ions |
Reference |
|---|
   1.1.1.12 | Cu2+ |
activates |
761551 |
| 1.1.1.12 | Fe2+ |
activates |
761551 |
| 1.1.1.12 | more |
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects |
761551 |
| 1.1.1.12 | Zn2+ |
a structural zinc ion is situated at a loop region located adjacent to the catalytic domain, where it is ligated by enzyme residues Cys108, Cys111, Cys114, and Cys122. The catalytically requisite zinc ion constitutes the second metal found in each monomer of LAD. This metal is coordinated by residues Cys53, His78, and Glu79, with a water molecule completing a near-tetrahedral coordination sphere |
712767 |
| 1.1.1.12 | Zn2+ |
catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, molecular docking studies |
712797 |
| 1.1.1.12 | Zn2+ |
required, the zinc ADH signature and conserved coenzyme binding motif are observed in the amino acid sequence of McXDH at positions 65-76 and 183-188 and are completely conserved among McXDH and XDHs from other yeasts and filamentous fungi |
761551 |
| 1.1.1.12 | Zn2+ |
structure analysis indicates that enzyme belongs to the family of Zn2+-containing, medium-chain alcohol dehydrogenases. Residues involved in Zn2+ binding are C55, H80, and E165. Thereis a second zinc-binding site C110, C113, C116, and C124 |
711121 |
| 1.1.1.12 | Zn2+ |
the Cys66, His91, Glu92, and Glu176 residues are involved in coordination of catalytic Zn2+ along with a water molecule |
740145 |
| 1.1.1.12 | Zn2+ |
two ions per subunit |
684627 |
| 1.1.1.12 | Zn2+ |
zinc metalloenzyme |
738728 |
