3.5.1.105: chitin disaccharide deacetylase
This is an abbreviated version!
For detailed information about chitin disaccharide deacetylase, go to the full flat file.
Word Map on EC 3.5.1.105
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3.5.1.105
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pyrococcus
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vibrio
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deacetylation
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chitinase
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synthesis
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horikoshii
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parahaemolyticus
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deacetylases
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n-acetyl
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thermococcus
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glucosamine
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n-acetylglucosamine
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hyperthermophilic
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chitinolytic
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furiosus
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glcnac-glcn
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rhizobium
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chitin-degrading
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kodakaraensis
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nodabc
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chitin-binding
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diagnostics
- 3.5.1.105
- pyrococcus
- vibrio
-
deacetylation
- chitinase
- synthesis
- horikoshii
- parahaemolyticus
- deacetylases
-
n-acetyl
- thermococcus
- glucosamine
- n-acetylglucosamine
-
hyperthermophilic
-
chitinolytic
- furiosus
-
glcnac-glcn
- rhizobium
-
chitin-degrading
- kodakaraensis
-
nodabc
-
chitin-binding
- diagnostics
Reaction
Synonyms
carbohydrate esterase family 4 chitin oligosaccharide deacetylase, CE family 4 COD, CE-14 deacetylase, ChbG, chitin disaccharide deacetylase, chitin oligosaccharide deacetylase, chitooligosaccharide deacetylase, chitooligosaccharide deacetylase homolog, COD, codA, Dac, Dacph, deacetylase DA1, diacetylchitobiose deacetylase, GlcNAc2 deacetylase, N,N'-diacetylchitobiose deacetylase, NodB, NodB homology domain-containing protein, Pa-COD, PF0354, PGTG_04950, Ph-Dac, PH0499, polysaccharide deacetylase, Sb-COD, Sbal_1411, Tk-Dac, TK1764, VC_1280, Vp-COD, VP2638, YdjC, YDJC deacetylase
ECTree
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Subunits
Subunits on EC 3.5.1.105 - chitin disaccharide deacetylase
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hexamer
homohexamer
additional information
comprised of two trimers. An intermolecular cleft is formed by two polypeptides in the trimeric assembly
hexamer
comprised of two trimers. An intermolecular cleft is formed by two polypeptides in the trimeric assembly
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
additional information
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the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
additional information
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the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
-
additional information
-
the Pyrococcus Dac enzyme forms a homohexamer composed of two trimers. A deep cleft exists between two polypeptides in each trimeric assembly, with the central Zn being chelated at the bottom by two His residues and one Asp residue. Determination, analysis and modelling of tertiary structure of Ph-Dac
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additional information
the enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains
additional information
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the enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains
additional information
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the enzyme comprises one polysaccharide deacetylase domain and two carbohydrate-binding domains
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