Literature summary for 3.5.1.105 extracted from

Nakamura, T.; Yonezawa, Y.; Tsuchiya, Y.; Niiyama, M.; Ida, K.; Oshima, M.; Morita, J.; Uegaki, K.
Substrate recognition of N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii (2016), J. Struct. Biol., 195, 286-293 .

Search for more literature for 3.5.1.105

Crystallization (Commentary)

Crystallization (Comment)	Organism
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
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

Crystallization (Comment)

Organism

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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the Ph-Dac crystal structure contains a phosphate ion bound to the metal ion, catalytic Zn2+	Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
N,N'-diacetylchitobiose + H2O	Pyrococcus horikoshii	-	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	Pyrococcus horikoshii DSM 12428	-	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	Pyrococcus horikoshii NBRC 100139	-	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	Pyrococcus horikoshii JCM 9974	-	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	Pyrococcus horikoshii ATCC 700860	-	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	Pyrococcus horikoshii OT-3	-	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O58235	-	-
Pyrococcus horikoshii ATCC 700860	O58235	-	-
Pyrococcus horikoshii DSM 12428	O58235	-	-
Pyrococcus horikoshii JCM 9974	O58235	-	-
Pyrococcus horikoshii NBRC 100139	O58235	-	-
Pyrococcus horikoshii OT-3	O58235	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii DSM 12428	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii NBRC 100139	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii JCM 9974	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii ATCC 700860	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii OT-3	N-acetyl-beta-D-glucosaminyl-(1->4)-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii DSM 12428	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii NBRC 100139	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii JCM 9974	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii ATCC 700860	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N,N'-diacetylchitobiose + H2O	-	Pyrococcus horikoshii OT-3	N-acetyl-beta-D-glucosaminyl-D-glucosamine + acetate	-	?
N-acetyl-D-glucosamine + H2O	-	Pyrococcus horikoshii	D-glucosamine + acetate	-	?
N-acetyl-D-glucosamine + H2O	-	Pyrococcus horikoshii DSM 12428	D-glucosamine + acetate	-	?
N-acetyl-D-glucosamine + H2O	-	Pyrococcus horikoshii NBRC 100139	D-glucosamine + acetate	-	?
N-acetyl-D-glucosamine + H2O	-	Pyrococcus horikoshii JCM 9974	D-glucosamine + acetate	-	?
N-acetyl-D-glucosamine + H2O	-	Pyrococcus horikoshii ATCC 700860	D-glucosamine + acetate	-	?
N-acetyl-D-glucosamine + H2O	-	Pyrococcus horikoshii OT-3	D-glucosamine + acetate	-	?

Subunits

Subunits	Comment	Organism
hexamer	dimer of trimers	Pyrococcus horikoshii
More	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	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
CE-14 deacetylase	-	Pyrococcus horikoshii
Dac	-	Pyrococcus horikoshii
N,N'-diacetylchitobiose deacetylase	-	Pyrococcus horikoshii
Ph-Dac	-	Pyrococcus horikoshii
PH0499	-	Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Pyrococcus horikoshii

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to carbohydrate esterase (CE) family 14	Pyrococcus horikoshii
metabolism	N,N'-diacetylchitobiose deacetylase (Dac) belongs to the CE-14 family and plays a role in the chitinolytic pathway in archaea by deacetylating N,N'-diacetylchitobiose (GlcNAc2), which is the end product of chitinase	Pyrococcus horikoshii
additional information	enzyme structure analysis and modelling, molecular dynamics simulation	Pyrococcus horikoshii