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3.2.1.6: endo-1,3(4)-beta-glucanase

This is an abbreviated version!
For detailed information about endo-1,3(4)-beta-glucanase, go to the full flat file.

Word Map on EC 3.2.1.6

Reaction

(Glcbeta(1-3))n
+
H2O
=
Laminaripentaose
 +
(Glcbeta(1-3))n-5

Synonyms

1,3-(4)-beta-glucanase (endoglucanase), 1,3-1,4-beta-glucanase EII (barley), 1,3-beta-D-glucanase, AFUA_1G05290, AFUA_2G14360, AFUA_4G13360, AFUA_5G02280, Agl9A, AkLam36, barley-beta-D-glucanase, beta-1,3-1,4 glucanase, beta-1,3-1,4-glucanase, beta-1,3-glucanase, beta-1,3:1,4 glucanase, beta-D-(1-3)-glucanase, beta-glucanase, bglBC1, CBM-CD, CC1G_01665, Cel8A, CelL, chitosanase, CMCase, CtLic26A, enda-beta-(1-3),(1-4)-glucanase, endo beta-1,3-glucanase IV, endo-1,3(4)-beta-D-glucanase, endo-1,3(4)-beta-glucanase, endo-1,3-1,4-beta-D-glucanase, endo-1,3-beta-D-glucanase, endo-1,3-beta-glucanase, endo-1,4-beta-glucanase, endo-beta-(1-3)-D-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-1,4-D-glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3-glucanase, endo-beta-1,4-glucanase, eng1, ENG16A, Eng2, Eng3, Eng4, Eng5, Engl1, Fsbeta-glucanase, GluA, H(A16-M), HdLam33, LAM, Lam16A, LamA, lamarinase, laminaranase, laminarinase, laminarinase 16A, laminarinase II, laminarinase Lam16A, LamR, LIC 1, Lic16A, Lic8H, Lichenase, More, nonlytic endo-beta-1,3-glucanase I, SsGlc, TcGlu2, TeEgl5A, Xyn10B

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.6 endo-1,3(4)-beta-glucanase

Crystallization

Crystallization on EC 3.2.1.6 - endo-1,3(4)-beta-glucanase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3-D structure, at 1.5 A resolution, of CtLic26A in complex with thiopentasaccharide. Crystals are in space group P2(1)2(1)2(1) with cell dimensions of a = 49.3 A, b = 63.0 A and c = 78.3 A and with a single molecule of CtLic26A in the asymmetric unit
-
homology modeling of structure. Amino acids Glu380, Gln383, Asp384, Tyr395, Ser712, and Arg713 present in the protein are of core importance for binding activities and these residues are having strong hydrogen bond interactions with beta-(1,3)-glucan
-
crystal structure of truncated Fsbeta-glucanase in complex with beta-1,3-1,4-cellotriose, resolution of 2.3 A
-
hanging-drop vapor-diffusion at room temperature, space group P2(1)2(1)2(1), cell parameters: a = 75.77 A, b = 88.76 A, c = 154.79 A. High-resolution crystal structure of the hybrid 1,3-1,4-beta-glucanase H(A16-M)E105Q/E109Q in complex with a beta-glucan tetrasaccharide
-
structure was solved at 1.34 A resolution using native sulfur SAD X-ray crystallography. Crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 38, b = 47, c = 152 A
-
X-ray crystallography screening of ligands bound nucleophile mutant E115S, to 1 A resolution. Laminariheptaose binds in an arch with the reducing and nonreducing ends occupying either side of the catalytic cleft of the enzyme. alpha-Laminariheptaosyl fluoride can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan. The cyclic laminariheptaose molecule is not completely planar and torsion angles at the glycosidic linkages fluctuate between two energy minima
to 1.95 A resolution, and molecular dynamics simulation studies. LamR is formed mostly by beta-sheets in a complex jelly roll topology that is conserved among members of glycosyl hydrolase family 16. It contains a relatively large number of salt bridges, which are not randomly distributed on the structure. They form clusters interconnecting beta-sheets of the catalytic domain. Structure reveals a glycerol molecule fortuitously bound to the active site of the enzyme molecule