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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.14 KCl 0.2-1 M KCl increases activity of ChiADELTA4 and ChiADELTA4 to 110% Thermococcus kodakarensis
3.2.1.14 NaCl 0.2-1 M NaCl increases activity of ChiADELTA4 and ChiADELTA4 to 110% Thermococcus kodakarensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.14 overexpression in Escherichia coli Thermococcus kodakarensis

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.14 ChiADELTA2 consits of chitin-binding domains ChBD2 and ChBD3 and catalytic domain B Thermococcus kodakarensis
3.2.1.14 ChiADELTA3 consits of chitin-binding domain ChBD1 and catalytic domain A Thermococcus kodakarensis
3.2.1.14 ChiADELTA4 consits only of catalytic domain B Thermococcus kodakarensis
3.2.1.14 ChiADELTA5 consits only of catalytic domain A Thermococcus kodakarensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.200 KCl 0.2-1 mM, 110% of initial activity Thermococcus kodakarensis
3.2.1.200 NaCl 0.2-1 mM, 110% of initial activity Thermococcus kodakarensis
3.2.1.201 KCl 0.2-1 mM, 110% of initial activity Thermococcus kodakarensis
3.2.1.201 NaCl 0.2-1 mM, 110% of initial activity Thermococcus kodakarensis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.14 Thermococcus kodakarensis
-
KOD1
-
3.2.1.200 Thermococcus kodakarensis Q9UWR7
-
-
3.2.1.201 Thermococcus kodakarensis Q9UWR7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.14
-
Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.201 62.7
-
substrate chitin, N-terminal catalytic domain, pH 5.0, 80°C Thermococcus kodakarensis
3.2.1.201 477
-
substrate ethylene glycol chitin, N-terminal catalytic domain, pH 5.0, 80°C Thermococcus kodakarensis
3.2.1.201 2490
-
substrate colloidal chitin, N-terminal catalytic domain, pH 5.0, 80°C Thermococcus kodakarensis
3.2.1.201 3160
-
substrate chitosan, 70% deacetylated, N-terminal catalytic domain, pH 5.0, 80°C Thermococcus kodakarensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.14 chitin + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose + ? major product ?
3.2.1.14 colloidal chitin + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose + ? major product ?
3.2.1.14 ethylene glycolchitin + H2O
-
Thermococcus kodakarensis ?
-
?
3.2.1.14 N,N',N'',N''', N'''',N'''''-hexaacetylchitohexaose + 2 H2O
-
Thermococcus kodakarensis 3 N,N'-diacetylchitobiose major product ?
3.2.1.14 N,N',N'',N''',N''''-pentaacetylchitopentaose + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose + N-acetyl-D-glucosamine major product ?
3.2.1.14 N,N',N'',N'''-tetraacetylchitotetraose + H2O
-
Thermococcus kodakarensis 2 N,N'-diacetylchitobiose major product ?
3.2.1.14 N,N',N''-triacetylchitotriose + H2O
-
Thermococcus kodakarensis N-acetyl-D-glucosamine + N,N'-diacetylchitobiose
-
?
3.2.1.14 partially N-acetylated chitosan + H2O chitosan 7B, 8B, 9B and 10B Thermococcus kodakarensis ?
-
?
3.2.1.201 chitin + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose + ? sole product of the N-terminal catalytic domain, the domain mainly hydrolyzes the second glycosidic bond from the nonreducing end of the oligomers ?
3.2.1.201 colloidal chitin + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose + ?
-
?
3.2.1.201 ethylene glycol chitin + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose
-
?
3.2.1.201 partially N-acetylated chitosan + H2O
-
Thermococcus kodakarensis N,N'-diacetylchitobiose
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.14 Tk-ChiA
-
Thermococcus kodakarensis
3.2.1.200 ChiA
-
Thermococcus kodakarensis
3.2.1.201 ChiA
-
Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.14 85
-
ChiADELTA4 Thermococcus kodakarensis
3.2.1.14 90
-
ChiADELTA5 Thermococcus kodakarensis
3.2.1.200 85
-
-
Thermococcus kodakarensis
3.2.1.201 85
-
-
Thermococcus kodakarensis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.14 80
-
ChiADELTA4: over 60 min in a pH range from 5-9, ChiADELTA5: over 60 min in a pH range from 4-9 Thermococcus kodakarensis
3.2.1.14 90
-
half-life of ChiADELTA5 is 5 min Thermococcus kodakarensis
3.2.1.14 100
-
half-life of ChiADELTA4 is more than 7 h Thermococcus kodakarensis
3.2.1.200 80
-
stable for 60 min Thermococcus kodakarensis
3.2.1.200 90
-
half-life 5 min Thermococcus kodakarensis
3.2.1.201 80
-
stable for 60 min Thermococcus kodakarensis
3.2.1.201 90
-
half-life 5 min Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.14 4.5
-
ChiADELTA4 Thermococcus kodakarensis
3.2.1.14 4.5 8 ChiADELTA5 Thermococcus kodakarensis
3.2.1.200 4.5
-
-
Thermococcus kodakarensis
3.2.1.201 4.5
-
-
Thermococcus kodakarensis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.200 5 9
-
Thermococcus kodakarensis
3.2.1.201 5 9
-
Thermococcus kodakarensis

General Information

EC Number General Information Comment Organism
3.2.1.200 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
3.2.1.201 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