3.5.1.105: chitin disaccharide deacetylase

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For detailed information about chitin disaccharide deacetylase, go to the full flat file.

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

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.1 In linear amides

                3.5.1.105 chitin disaccharide deacetylase

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Results	in table
1471	AA Sequence
25	Application
16	Cloned(Commentary)
6	Crystallization (Commentary)
3	Disease/ Diagnostics
11	Expression
89	General Information
9	Inhibitors
5	kcat/KM [mM/s]
9	KM Value [mM]
6	Localization
2	Metals/Ions
9	Molecular Weight [Da]
47	Natural Substrates/ Products (Substrates)
159	Organism
2	PDB ID
12	pH Optimum
1	pH Range
4	pH Stability
1	pI Value
41	Protein Variants
13	Purification (Commentary)
1	Reaction
77	Reference
7	Source Tissue
9	Specific Activity [micromol/min/mg]
150	Substrates and Products (Substrate)
35	Subunits
169	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
3	Temperature Range [°C]
7	Temperature Stability [°C]
3	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.5.1.105 - chitin disaccharide deacetylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structure is determined at resolutions of 1.54 A

Pyrococcus furiosus

Q8U3V1

727488

the native enzyme and its selenomethionine derivative are crystallized and analyzed in the presence and absence of cadmium ion

Pyrococcus furiosus

Q8U3V1

731090

crystal structure is determined at resolutions of 2.0 A

Pyrococcus horikoshii

O58235

727488

hanging drop vapor-diffusion method, the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue

Pyrococcus horikoshii

O58235

745652

purified enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose, hanging drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 10 mM MPG, 20 mM Tris-HCl, pH 8.1, and 150 mM NaCl, with 0.001 ml of reservoir solution containing either 0.4 M ammonium phosphate (reservoir 1) or 100 mM sodium acetate, pH 4.6, 10 mM CoCl2, and 1 M 1,6-hexanediol (reservoir 2), equilibration against 0.4 ml of reservoir solution, 20°C, X-ray diffraction structure determiantion and analysis at 1.8-1.9 A resolution, modelling

Pyrococcus horikoshii

O58235

745652

purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM sodium phosphate, pH 7.0, with an equal volume of reservoir solution containing 0.1 M Tris-HCl, pH 7.0, 10% w/v PEG 8000, and 0.2 M MgCl2, 4 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.35 A resolution

Vibrio parahaemolyticus

A6P4T5

733875