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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.14 | overexpression in Escherichia coli | Thermococcus kodakarensis |
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 |
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 |
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 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.14 | - |
Thermococcus kodakarensis |
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 |
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 | - |
? |
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 |
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 |
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 |
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 |
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 |
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 |