EC Number   |
Metals/Ions |
Reference |
|---|
   3.2.1.6 | Ca2+ |
1 mM, 1.2fold increase in activity |
744059 |
| 3.2.1.6 | Ca2+ |
1 mM, 130% of initial activity |
745016 |
| 3.2.1.6 | Ca2+ |
32% increase of activity by 10 mM |
136376 |
| 3.2.1.6 | Ca2+ |
activates, 5 mM Ca2+ increases the lichenase activity by 15%. Ca2+ increases the heat stability of the lichenase activity |
729478 |
| 3.2.1.6 | Ca2+ |
enzyme N-terminal module CBM54 substrate binding promiscuity suggests multiple binding sites, some of them being Ca2+-dependent. The Ca2+-independent sites for avicel, pustulan and chitosan are localized to the spontaneously split-off N-terminal part of 8 kDa of CBM54. Determination of binding constants and binding capacity for substrates tested, in presence and absence of Ca2+ |
716160 |
| 3.2.1.6 | Ca2+ |
identification of calcium ions bound to each monomer, in equivalent sites of each polypeptide chain in the asymmetric unit cell, and displaying the same coordination patterns. Coordination of the calcium ion is 6fold, and involves Gly60 of main chain, Asp248, main chain and side chain, Glu18 of main chain, and two water molecules. Crystallization data |
716020 |
| 3.2.1.6 | Ca2+ |
slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity. Calcium ion has a general stabilizing effect on Bacillus beta-1,3-1,4 glucanases. Calcium is bound to the backbone carbonyl oxygens of Pro9, Gly45, Asp207 and carboxylate oxygen of Asp207 and two water molecules |
729343 |
| 3.2.1.6 | Co2+ |
1 mM, 1.4fold increase in activity |
744059 |
| 3.2.1.6 | Co2+ |
1 mM, 119% of initial activity |
744121 |
| 3.2.1.6 | Co2+ |
1 mM, 143% of initial activity |
745016 |
