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3.2.1.179: gellan tetrasaccharide unsaturated glucuronosyl hydrolase

This is an abbreviated version!
For detailed information about gellan tetrasaccharide unsaturated glucuronosyl hydrolase, go to the full flat file.

Word Map on EC 3.2.1.179

Reaction

beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp
+
H2O
=
5-dehydro-4-deoxy-D-glucuronate
 +
beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp

Synonyms

CaUGL, CA_C0359, More, SagUGL, UGL, unsaturated glucuronyl hydrolase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.179 gellan tetrasaccharide unsaturated glucuronosyl hydrolase

Crystallization

Crystallization on EC 3.2.1.179 - gellan tetrasaccharide unsaturated glucuronosyl hydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized at 20°C from a droplet containing 56% 2-methyl-2,4-pentanediol, 0.1 M NaCl, 0.1 M glycine/NaOH pH 8.2 and 0.1 M dithiothreitol using the hanging-drop vapour-diffusion method. The crystals are hexagonal and belonged to space group P6122 or P6522, with unit-cell parameters a = b = 102.8, c = 223.4 A. Diffraction data to 2.4 A are collected from a single crystal
crystals are obtained by using hanging drop vapor diffusion and microseeding, wild-type enzyme, mutant enzyme D88N and mutant enzyme D88N in complex with beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
sitting-drop vapor duffusion method, X-ray crystallographic structure of the enzyme at 1.8 A resolution
vapor diffusion method, demonstration of substrate recognition mechanism of the unsaturated glucuronyl hydrolase by determining the X-ray crystallographic structure of its substrate-enzyme complexes (D88N/DELTAGlcA-Glc-Pha-Glc and D99N/DELTAGlcA-GlcNAc). The tetrasaccharide-enzyme complex demonstrates that at least four subsites are present in the active pocket
partially purified recombinnat enzyme, hanging-drop vapor-diffusion method, mixing 0.002 ml 7.5 mg/ml protein solution with 0.002 ml reservoir solution consisting of 0.1 M Tris, pH 7.75, 16% w/v PEG 4000, 21°C, X-ray diffraction structure determination and analysis at 1.6 A resolution, modelling
purified recombinant enzyme mutants D115N and D115N/K370S, sitting drop vapor diffusion, 20 mg/ml and 40 mg/ml protein solution, respectively, is mixed with an equal volumes of reservoir solution. The reservoir solution for mutant D115N crystallization contains 1.5 M ammonium sulfate and 0.1 M Tris-HCl, pH 9.0, D115N crystals are grown at 20°C for a week. The reservoir solution for mutant D115N/K370S crystallization contains 40% ethylene glycol, 0.5 mM dithiothreitol, and 0.1 M Tris-HCl, pH 7.0, D115N/K370S is crystallized at 20°C for 2 months. X-ray diffraction structure determination and analysis at 2.00 A and 1.79 A resolution, respectively