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3.2.1.131: xylan alpha-1,2-glucuronosidase

This is an abbreviated version!
For detailed information about xylan alpha-1,2-glucuronosidase, go to the full flat file.

Word Map on EC 3.2.1.131

Reaction

(4O-Me)GlcAalpha(1-2)[(Xylbeta(1-3))n](Xylbeta(1-3)m)
+
H2O
=
Xylbeta(1-3)m+n
+
4-O-methyl-alpha-D-glucuronic acid

Synonyms

Agu1, Agu115, Agu115A, Agu67A, AguA, alpha-(1->2)-glucuronidase, alpha-glucuronidase, AugA, AxyAgu115A, BtGH115A, DEG75-AG, GH115, GH115 4-O-methyl-alpha-glucuronidase, GH115 alpha-glucuronidase, GH67, GlcA115A, glucuronidase, 1,2-alpha-, ScAGU115, Sde_1755, Theth_0154, xylanolytic alpha-glucuronidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.131 xylan alpha-1,2-glucuronosidase

Crystallization

Crystallization on EC 3.2.1.131 - xylan alpha-1,2-glucuronosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using 19% (w/v) PEG3350, 0.2 M sodium citrate, pH 5.5
-
vapor phase diffusion using the hanging drop method, 250 mM MgCl2 and 20% v/v ethylene glycol with 15% w/v polyethylene glycol 3350 as prcipitant at 20°C, triclinic space group P1 with a: 69.9 A, b: 74.7 A, c: 87.6 A, alpha: 115.2°, beta: 93.1° and gamma: 109.3°
-
hanging drop method at 20°C, 10 mg/ml enzyme solution mixed with an equal volume of reservoir solution, containing 14% w/v polyethylene glycol 4000, 12% v/v isopropyl alcohol and 0.1 M sodium citrate, pH 5.5, tetragonal space group P41212 with a and b: 74.6 A and c: 330.3 A
-
two crystal forms, form T1 is obtained by the vapour-diffusion method using polyethylene glycol as precipitant and 2-propanol as organic additive, tetragonal space group P41212 or P43212 with a and b: 76.1 A and c: 331.2 A, form M1 at slightly lower pH and lower concentration of 2-propanol, monoclinic space group P21 with a: 65.8 A, b: 127.4 A, c: 96.6 A and beta: 97.9°
-
structural analysis. Residue E288 acts at the catalytic proton donor, D367 and E395 are likely nucleophilic bases
structure reveals a five-domain architecture, with an additional insertion C+ domain that has significant impact on the domain arrangement of the protein monomer and its dimerization. The participation of domain C+ in substrate binding is supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. In addition to Asp335, residue Glu216 is essential for the catalytic activtiy
sitting drop vapor diffusion method, using 16% (w/v) PEG 2000 MME and 0.1 M Tris pH 7.0
-