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3.2.1.132: chitosanase

This is an abbreviated version!
For detailed information about chitosanase, go to the full flat file.

Word Map on EC 3.2.1.132

Reaction

2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose
+
H2O
=
2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranose
+
2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-amino-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose

Synonyms

actase, AsChi, BspCsnMN, Cel7A, Cel8A, ChA, CHI, ChiN, Chit A, Chit B, chitosan N-acetylglucosaminohydrolase, chitosanase, chitosanase 1, chitosanase CsnA, chitosanase EAG1, chitosanase II, chitosanase OU01, ChiX, CHO, Cho-GG, ChoK, Chs1, Csn, CSN-174, CSN-7M, Csn-PD, Csn1, Csn2, CsnA, CsnB, CsnM, CSNMHKI, CsnN174, CsnTS, csnw2, Cto1, CtoA, Culf-Z, endo-acting chitinase, endo-chitosanase, endochitosanase, family 46 chitosanase, GH-75 chitosanase, GsCsn46A, ImmB-Z, MH-K1 chitosanase, More, mschito, N174 chitosanase, PgChP, SACTE_5457, SCO0677, StrCSN1, StrCSN2, TKU032 chitosanase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.132 chitosanase

Crystallization

Crystallization on EC 3.2.1.132 - chitosanase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determined at 1.5 A resolution in the active form and at 2.0 A resolution in the inactive form. Hanging-drop vapor-diffusion method
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two different crystal forms, ChoK-a and ChoK-i are obtained at pH 6.4 and pH 3.7, respectively. ChoK-a crystals belong to space group P2(1)2(1)2(1). From the unit-cell parameters, a = 70.8 A, b = 98.1 A, c = 115.8 A. The number of protein molecules in the asymmetric subunit is estimated to be two. The crystal diffracts well to 1.5 A resolution. The ChoK-i crystal belongs to space group I222, with unit-cell parameters a = 85.1 A, b = 91.1 A, c = 131.5 A. There is one molecule in the asymmetric subunit and the resolution is restricted to 2.0 A
-
in complex with hexaglucosamine, hanging drop vapor diffusion method, using 0.05 M KH2PO4 and 23% (w/v) PEG 8000 using 0.7 M NaCl as the reservoir at 15°C
crystal structure of mutant enzyme K218P
sitting drop vapor diffusion method at 20°C. The crystal structure of mutant K218P reveals that the main chain and side chain structures of the loop comprising Lys218 are effected by the mutation. It is concluded that the flexible loop comprising Lys128 plays an important role in substrate binding
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sitting drop vapour diffusion method at 20°C, orthorhombic space group P21212, two globular upper and lower domains which generate the active site cleft for the substrate binding
hanging drop vapor diffusion at 15°C
hanging drop crystallization with 30 mg/ml protein in 20 mM acetate, pH 5.5 mixed with 0.1 volume of a 0.5 M potassium phosphate, 20% w/v PEG 8000 solution, monoclinic space group P21
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sitting drop vapor diffusion method, using 10% (w/v) MEPEG 5K, 300 mM tetramethylammonium chloride, and 100 mM Bis-Tris, pH 6.5, at 4°C
the substrate binding cleft is composed of six monosaccharide binding subsites
-