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Literature summary for 3.2.1.200 extracted from

  • Tanaka, T.; Fukui, T.; Imanaka, T.
    Different cleavage specificities of the dual catalytic domains in chitinase from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 (2001), J. Biol. Chem., 276, 35629-35635.
    View publication on PubMed

Metals/Ions

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

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q9UWR7
-
-

Synonyms

Synonyms Comment Organism
ChiA
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Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
-
Thermococcus kodakarensis

Temperature Stability [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
Thermococcus kodakarensis

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 9
-
Thermococcus kodakarensis

General Information

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