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3.2.1.52: beta-N-acetylhexosaminidase

This is an abbreviated version!
For detailed information about beta-N-acetylhexosaminidase, go to the full flat file.

Word Map on EC 3.2.1.52

Reaction

(N-acetyl-D-glucosamine)4
+ 3 H2O = 4 2-(acetylamino)-2-deoxy-beta-D-glucopyranose

Synonyms

2-acetamido-2-deoxy-beta-D-glucoside acetamidodeoxyglucohydrolase, 3-beta-N-acetylglucosaminidase, 65 kDa epididymal boar protein, Am2301, Am2446, At1g65600/F5I14_13, beta-acetylaminodeoxyhexosidase, beta-acetylhexosaminidase, beta-acetylhexosaminidinase, beta-D-hexosaminidase, beta-D-N-acetylhexosaminidase, Beta-GlcNAcase, beta-glucosidase, beta-HEX, beta-HexNAcase, beta-hexosaminidase, beta-hexosaminidase A, beta-hexosaminidase B, beta-hexosaminidase I, beta-hexosaminidase II, beta-N-acetyl-D-glucosaminidase, beta-N-acetyl-D-hexosaminidase, beta-N-acetyl-hexosaminidase, beta-N-acetylgalactosaminidase, beta-N-acetylglucosaminidase, Beta-N-acetylhexosaminidase, beta-N-acetylhexosaminidase A, beta-N-acetylhexosaminidase B, beta-Nacetylhexosaminidase S, beta-NAGase, beta-NAHA, Beta-NAHASE, bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase, BmCHI-h, BmGlcNAcase 1, BmGlcNAcase 2, BmNPV CHIA, CbsA, Chi-I, Chi-II, chitobiase, chitobiase 2, CpGV V-CHIA, dispersin B, DmHEXA, DmHEXB, DspB, EC 3.2.1.29, EC 3.2.1.30, endo-beta-N-acetylglucosaminidase, EXC1Y, EXC2Y, exo-acting chitinase, exo-beta-D-N-acetylglucosaminidase, exo-beta-hexosaminidase, exo-type beta-N-acetylhexosaminidase, exochitinase, F3F20.4 protein, FDL, GH84C, GlcNAcase, Hex, Hex A, Hex B, Hex-1, Hex1, Hex2, Hex20, Hex4, HexB, HexD, HEXDC, hEXO1, HEXO2, HEXO3, hexosaminidase, hexosaminidase A, hexosaminidase B, hexosaminidase D, hHexA, lacto-N-biosidase, lnba, lysosomal beta-hexosaminidase, More, N-acetyl-beta-D-hexosaminidase, N-acetyl-beta-glucosaminidase, N-acetyl-beta-hexosaminidase, N-acetylglucosaminidase, N-acetylhexosaminidase, NAG-68, NAG-B, NAG1, NAG2, Nag3, NagA, NAGase, NagJ, NagZ, NAHA, NAHase, neutral hexosaminidase C, O-GlcNAcase, Pcb-NAHA1, Sfhex, SSO3039, StrH, zymocin alpha-subunit

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.52 beta-N-acetylhexosaminidase

Crystallization

Crystallization on EC 3.2.1.52 - beta-N-acetylhexosaminidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.0 M ammonium sulfate, 20% (w/v) PEG 3350, and 100 mM HEPES, pH 8.0
hanging-drop vapour-diffusion method, crystals of primitive monoclinic and primitive tetragonal crystal forms, to resolutions of 3.2 and 2.4 A, respectively
complex of Bacteroides thetaiotaomicron BtGH84 with the inhibitor, analysis at 2 A resolution, data quality and structure refinement statistics shown, unsaturated ring is distorted away from its favoured solution phase conformation indicating potential for improved inhibitor potency
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purified recombinant enzyme fragments: GH84C catalytic module fragment, and GH84C fragment comprising the catalytic module and the adjacent CBM32, as well as a fragment with the FN3 module, hanging drop vapor diffusion method, 10-25 mg/ml protein in 20 mM Tris-HCl, pH 8.0, is mixed with precipitant solution containing 0.1 M Tris-HCl, pH 7.5, 0.1 M MgCl2, 15% w/v PEG 4000, or 0.1 M sodium acetate, pH 3.5, 4% w/v PEG 8000, at 18°C, structure determination and analysis by combination of small angle X-ray scattering and X-ray crystallography at 1.8-3.3 A resolution
hanging-drop method, crystal structure of beta-hexosaminidase B, alone at 2.4 A and in complex with the mechanistic inhibitor GalNAc-isofagomine at 2.2 A or N-acetyl-beta-D-glucosamine-thiazoline at 2.5 A resolution
hanging-drop vapour-diffusion method, crystal structure of a complex of beta-hexosaminidase B with a transition state analogue inhibitor 1-acetamido-2-deoxy-D-glucono-1,5-lactone at 2.3 A resolution
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hexosaminidase B, space group P6122 i.e. enantiomorph, 3.2 A resolution
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vapor diffusion method
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native enzyme andd in complex with TMG-chitotriomycin, both to 2.1 A resolution. Enzyme displays large conformational changes linked to an open-close mechanism at the entrance of the active site, which is characterized by the lid residue, Trp448. Structure shows a homodimeric enzyme with the two monomers in the adjacent asymmetry units. Each monomer is N-glycosylated at Asn164 and Asn375. All of the 12 cysteine residues of each monomer contribute to the intradisulfide bonds
purified recombinant wild-type isozymes Hex1 and Hex2, and mutant Hex1-DELTAC, and of isozymes in complex with N-acetyl-beta-D-glucosamine and N-acetyl-beta-D-galactosmaine, by hanging drop vapor diffusion method, mixing 0.001 ml of protein solution, with 10 mg/ml protein in 10 mM HEPES-sodium buffer, pH 7.4, 150 mM NaCl, 10 mM 2-mercaptoethanol, with 0.001 ml of precipitant containing 0.2 M (NH4)2SO4, 20% w/v PEG 2000 and 0.1 M sodium acetate buffer, pH 4.6, X-ray diffraction structure determination and analysis at 1.6-1.9 A resolution, molecular replacement method
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2.1 A crystal structure of the N-terminal domain of StrH, residues Glu175-Lys642, complexed with N-acetylglucosamine. It adopts an overall structure similar to other GH20 enzymes, a (beta/alpha)8 TIM-barrel with the active site residing at the center of the beta-barrel convex side
H-bonding interactions of Hex with N-acetylglucosamine-thiazoline
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hanging-drop vapour-diffusion method. Structure of beta-hexosaminidase to 2.2 A resolution, complex between the cyclic intermediate analogue N-acetylglucosamine-thiazoline and beta-hexosaminidase to 2.1 A resolution
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