EC Number   |
Metals/Ions |
Reference |
|---|
   4.2.3.38 | KCl |
only weakly influences GDP conversion with the ag1 enzyme causing a 2fold activation at 100 mM KCl, but the monovalent cation has no effect with FDP as substrate |
694926 |
| 4.2.3.38 | Mg2+ |
activates, saturation with Mg2+ is reached at 5 mM, and no apparent inhibition of catalysis occurs up to 100 mM |
694926 |
| 4.2.3.38 | Mg2+ |
required |
730976 |
| 4.2.3.38 | Mn2+ |
activates, but Mn2+ at concentrations higher than 1 mM results in a decline of activity with either substrate |
694926 |
| 4.2.3.38 | more |
the activity of recombinant ag1 requires a divalent cation cofactor, Mg2+ or Mn2+, which is employed to neutralize the negative charge of the diphosphate leaving group in the substrate ionization step of the reaction sequence. Mg2+ is more efficient in catalysis than is Mn2+. With GDP as substrate, however, Mn2+ at 0.5 mM yields a 4fold higher rate of monoterpene synthase activity compared to Mg2+ at concentrations up to 50 mM |
694926 |
