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3.2.1.39: glucan endo-1,3-beta-D-glucosidase

This is an abbreviated version!
For detailed information about glucan endo-1,3-beta-D-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.39

Reaction

Laminariheptaose
+ 3 H2O =
laminaritriose
 + 2 laminaribiose

Synonyms

(1-3)-beta-D-glucan endohydrolase, (1-3)-beta-D-glucanase, (1-3)-beta-glucanase GI, (1->3)-beta-glucan endohydrolase, (1->3)-beta-glucan endohydrolase BGN13.1, (1->3)-beta-glucan endohydrolase GI, (1->3)-beta-glucan endohydrolase GII, (1->3)-beta-glucan endohydrolase GIII, (1->3)-beta-glucan endohydrolase GIV, (1->3)-beta-glucan endohydrolase GV, (1->3)-beta-glucan endohydrolase GVI, (1->3)-beta-glucanase, (1->3)-beta-glucanase A1, (1->3)-beta-glucanase BGN13.1, (1->3)-beta-glucanase isoenzyme GI, (1->3)-beta-glucanase isoenzyme GII, (1->3)-beta-glucanase isoenzyme GIII, (1->3)-beta-glucanase isoenzyme GIV, (1->3)-beta-glucanase isoenzyme GV, (1->3)-beta-glucanase isoenzyme GVI, (13)-beta-glucan 3-glucanohydrolase, (13)-beta-glucan endohydrolase, 1,3-beta-D-glucanase, 1,3-beta-glucan 3-glucanohydrolase, 1,3-beta-glucan hydrolase, 1,3-beta-glucanase, 1,3-beta-glucanase I, Acidic beta-1,3-glucanase, acidic endo-beta-1,3-glucanase, AkLam36, Anther-specific protein A6, Ban-Gluc, Basic beta-1,3-endoglucanase BGN13.1, Basic beta-1,3-glucanase, beta-(1-3)-glucanase, beta-1,3 glucanase, beta-1,3-D-glucanase, beta-1,3-endoglucanase, Beta-1,3-endoglucanase GI, Beta-1,3-endoglucanase GII, Beta-1,3-endoglucanase GIII, Beta-1,3-endoglucanase GIV, Beta-1,3-endoglucanase GV, Beta-1,3-endoglucanase GVI, Beta-1,3-endoglucanase, basic, beta-1,3-glucan hydrolase, beta-1,3-glucanase, beta-1,3-glucanase I, beta-1,3-glucanase II, beta-glucanase, Bgl, Bgl2, Bgl64A, BglF, BglII, BglS27, Bglu50A, Bgt17AE158A, CaENG, callase, CC1G_04051, CcGluE, Cel17A, DEHA2G18766g, DEHA2G18766p, EGase1, EGase2, EGase3, endo-(1,3)-beta-D-glucanase, endo-(1-3)-beta-glucanase, endo-(13)-beta-D-glucanase, endo-1,3-beta-D-glucanase, endo-1,3-beta-glucanase, endo-1,3-beta-glucosidase, endo-1,3-glucanase, endo-1,3;4-beta-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-D-glucanase, endo-beta-1,3-glucanase, endo-beta-1->3-glucanase, endo-type beta-1,3-glucanase, Endo23, Eng, eng1, ENG16A, Eng2, Eng2 protein, EngA, Engl1, exo-beta-1,3-glucanase, Fra e 9.01 allergen, Gbl2a, Gbl2b, Gbl2c, Gbl2d, Gbl2e, Gbl2f, Gbl3, Gfa, GH family 81 beta-1,3-glucanase, GLU, Glu1, GluA, GLUB20-2, glucan endo-1,3-beta-glucosidase, Glucanase GLA, Glucanase GLB, glucanase LIV, glucanase Lo, GLUD2, HdLam33, kitalase, LAM, Lam81A, LamA, laminaranase, laminarinase, Lic16A, lytic beta-(1-3)-glucanase I, lytic beta-(1-3)-glucanase II, Mo enzyme, More, oligo-1,3-glucosidase, OsGlu1, OsGlu2, PCEng2p, PfLamA, PpGns1, PR-2B, PR-35, PR-36, PR-37, Rv0315, SLam, SpsLamIV, TLam, TmLam, VIT_05s0077g01150, VIT_205s0077g01150, VIT_206s0061g00120, VIT_208s0007g06060, YlCrh1Sp, YlCrh2Sp, zerzaust, ZET, ZgLamA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.39 glucan endo-1,3-beta-D-glucosidase

Crystallization

Crystallization on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure homology modelling
-
in complex with laminarihexaose, single wavelength anomalous dispersion method, using a Na2AuCl4 derivative
to 1.66 A resolution, and modeling of laminarihexaose into the substrate-binding cleft. The substrates bind to the subsites -1 to -3 with the highest affinity, while the part bound to the reducing end will be hydrolyzed. Comparison of the endo-1,3-beta-glucanase catalytic domain with other known GH16 enzyme structures
enzyme possesses the eightfold beta/alpha architecture typical for family 17 glycoside hydrolases
-
structure of Rv0315 at 1.70 A resolution. Rv0315 is an inactive beta-1,3-glucanase of the glycoside hydrolase 16 (GH16) family. Rv0315 has a large open groove, and this particular topology cannot bind oligosaccharide chains in solution, thus explaining the lack of detectable hydrolytic activity towards its substrate
hanging drop vapour diffusion method with 0.1 M Tris-HCl (pH 8.0), 1.5 M ammonium sulfate, 0.1 M sodium chloride, and 1% (v/v) ethanol
-
sitting drop vapor diffusion method, using 1.2 M di-ammonium tartrate pH 7.0
modeling of structure and docking studies of glucanase inhibitor protein from Phytophthora capsici. Inhibition by glucanase inhibitor protein is mainly caused by recognition of an arginine as well as an isoleucine residue during the interaction of the two proteins
-
hanging drop vapour diffusion technique at 20°C, crystal structure is determined at 2.1 A resolution by molecular replacement
to 2.1 A resolution, determination by molecular replacement. Structure reveals a kink of six residues at the entrance of the catalytic cleft
purified recombinant detagged wild-type and selenomethionine-labeled enzymes, sitting drop vapour diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, with 0.001 ml of precipitant solution containing 200 mM Li2SO4, 30% w/v PEG 4000, 100 mM Tris-HCl, pH 8.5, or 160 mM Li2SO4, 24% w/v PEG 4000, 80 mM Tris-HCl, pH 8.5, 6% v/v 2-methyl-2,4-pentanediol, 2-4 weeks, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
the overall structure of the Lam81A monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Residues Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557
purified recombinant His-tagged mutant E259A in complex with laminarihexose, hanging drop vapour diffusion, mixing of 0.0015 ml of 7 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.0015 ml of reservoir solution containing 0.1 M sodium citrate, pH 5.6, 0.2 M ammonium acetate, 24% PEG 8000, 21°C, 2-7 days, crystals in form of bunched needles, single and larger crystals by use of streak-seeding, X-ray diffraction structure determination and analysis at 1.55-1.68 A, 3G and 7G crystal structures by molecular replacement
two different crystal forms: higher density and lower density determined at 1.40 A and 1.26 A resolution, respectively. The crystal structures reveal an unusual packing mode, clearly visible in the LD structure, caused by the presence of the C-terminal His6 tag, which extends from the compact fold of the enzyme molecule and docks in the catalytic cleft of a neighbouring molecule. In this way, an infinite chain of His-tag-linked protein molecules is formed along the c direction. Purified recombinant His-tagged enzyme by hanging drop vapour diffusion method, mixing of 0.0015 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.0015 ml of reservoir solution containing 0.1 M sodium acetate, pH 4.6, 0.2 M ammonium acetate, 25-30% PEG 4000, 21°C, 2 days, X-ray diffraction structure determination and analysis, modelling
catalytic domain, to 1.5 A resolution. The overall structure contains two antiparallel six- and seven-stranded beta-sheets stacked in a beta-sandwich jelly-roll motif. The active-site cleft of the enzyme shows the closure of one end primarily caused by two protruding loop insertions and two key residues, Y38 and Y134
small angle X-ray scattering data and homology modeling. Enzyme displays a multi-domain structural architecture of a V-shape envelope with a catalytic domain flanked by two carbohydrate-binding modules
purified recombinant His-tagged wild-type and mutant enzymes, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein with 0.002 ml reservoir solution containing 24% PEG 3350 and 100 mM sodium citrate, pH 5.2, 4°C, crystals of enzyme mutant E269S in complex with laminarin oligosaccharides are obtained from 0.002 ml of 13.3 mg/ml protein and 5 mM of purified hexasaccharides,with 0.001 ml of reservoir solution containing 100 mM sodium malonate, imidazole, and boric acid (MIB-buffer), pH 4.0, and 19% of PEG 1500 in hanging drops at 20°C. Single crystals of mutant E269S in complex with MLG trisaccharides are obtained from mixing 0.002 ml 11.7 mg/ml of protein, 0.04% w/v of MLG degradation products with 0.001 ml of reservoir solution containing 100 mM MIB buffer, pH 4.0, 17% of PEG 1500, and 10% of glycerol in hanging drops at 12°C, X-ray diffraction structure determination and analysis at 1.13-1.45 A resolution, molecular replacement method