EC Number   |
Metals/Ions |
Reference |
|---|
  4.2.3.128 | Mg2+ |
required |
705783, 713839, 747877 |
| 4.2.3.128 | Mg2+ |
required, enzyme CoTPS2 has the conserved aspartate-rich motif (DDXXD) and NSE/DTE motifs that chelate divalent metal ions, typically Mg2+, in the C-terminal domain |
743000 |
| 4.2.3.128 | Mg2+ |
required, maximal activities at Mg2+ concentrations of 1 to 10 mM |
720729 |
| 4.2.3.128 | Mg2+ |
required, substitution of Mg2+ with Mn2+ as the divalent metal ion shifts the product profile of Cop4 to germacrene D, disfavoring subsequent ring closures that produce the cadinyl cation and its tricyclic descendents. Two consensus sequences - an aspartate rich DDXXD/E and a NSE/DTE motif - located at the entrance of the active site coordinate a trinuclear Mg2+ cluster that ligands the diphosphate moiety of the isoprenoid substrate, positions the isoprenyl chain in the binding pocket and triggers closure of the active site along with diphosphate cleavage to generate an initial transoid, allylic carbocation |
714733 |
| 4.2.3.128 | Mn2+ |
activates, naximally at concentrations of 1 mM or less |
720729 |
| 4.2.3.128 | Mn2+ |
substitution of Mg2+ with Mn2+ as the divalent metal ion shifts the product profile of Cop4 to germacrene D, disfavoring subsequent ring closures that produce the cadinyl cation and its tricyclic descendents |
714733 |
| 4.2.3.128 | more |
the enzyme contains the metal-binding DDXXD motif |
713839 |
| 4.2.3.128 | NaCl |
does not affect the product specificity of Cop4 significantly at 1 M |
714733 |
