EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.11.7 | Ba2+ |
activation |
36013, 36021, 36024, 36027 |
| 3.4.11.7 | Ca2+ |
- |
683663 |
| 3.4.11.7 | Ca2+ |
7.3fold increase of ratio of turnover number to Km-value for the wild-type enzyme. Activity of mutant enzyme H450F is not measurable in absence of Ca2+. His450 together with Ca2+ may contribute to substrate specificity |
654574 |
| 3.4.11.7 | Ca2+ |
activates |
663456, 665074, 665110, 665570 |
| 3.4.11.7 | Ca2+ |
activates activity with some substrates, decreases activity with other substrates, required for activity with Asp-/Glu-substrates, regulatory function and influence on substrate specificity |
665723 |
| 3.4.11.7 | Ca2+ |
activates, best at 1 mM, substrate-specific activation |
663609 |
| 3.4.11.7 | Ca2+ |
activation |
35016, 35868, 36013, 36018, 36020, 36021, 36024, 36026, 36027, 36030 |
| 3.4.11.7 | Ca2+ |
each APA monomer contains one Ca2+ atom, Ca2+ (from 0 to 4 mM) increases the activity of the wild type enzyme |
696103 |
| 3.4.11.7 | Ca2+ |
glutamate specific enzyme |
36026 |
| 3.4.11.7 | Ca2+ |
localized at the bottom of the S1 subsite, activates the enzyme and plays a key role of Arg878 together with Ca2 + in APA substrate specificity for N-terminal acidic amino acid residues by ensuring the optimal positioning of acidic substrates during catalysis. The Ca2+ atom interacts with the acidic side chains of Asp213 and Asp218, the carbonyl group of Glu215 and three water molecules, one of them being engaged in a hydrogen bond with the negatively charged carboxylate side chains of the inhibitors. Ca2+ activation profile of purified recombinant wild-type and mutated His-mAPAs, using an acidic substrate alpha-L-glutamyl-beta-naphthylamide, overview. Enzyme residue Arg878 does not contribute to Ca2+ binding in the S1 subsite |
755153 |
