Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | 0.2-1 mM, 110% of initial activity | Thermococcus kodakarensis | |
NaCl | 0.2-1 mM, 110% of initial activity | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | Q9UWR7 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
ChiA | - |
Thermococcus kodakarensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
- |
Thermococcus kodakarensis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
stable for 60 min | Thermococcus kodakarensis |
90 | - |
half-life 5 min | Thermococcus kodakarensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.5 | - |
- |
Thermococcus kodakarensis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5 | 9 | - |
Thermococcus kodakarensis |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme has a multidomain structure containing dual catalytic domains and triple chitin-binding domains.The N-terminal catalytic domain mainly hydrolyzes the second glycosidic bond from the nonreducing end of the oligomers, whereas the C-terminal domain randomly hydrolyzes glycosidic bonds other than the first bond from the nonreducing end. Both catalytic domains form diacetylchitobiose as a major end product and possess transglycosylation activity. The N-terminal catalytic domain exclusively liberates diacetylchitobiose, whereas reactions with the C-terminal domain lead to N-acetyl-chitooligosaccharides of various lengths. A synergistic effect is observed when chitin is degraded in the presence of both catalytic domains | Thermococcus kodakarensis |