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3.2.1.73: licheninase

This is an abbreviated version!
For detailed information about licheninase, go to the full flat file.

Word Map on EC 3.2.1.73

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beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranose
+ 4 H2O = 5 beta-D-glucopyranose

Synonyms

(1,3)(1,4)-beta-D-glucan-4-glucanohydrolase, (1->3,1->4)-beta-glucanase isoenzyme EII, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, 1,3-1,4-beta-D-glucan glucanohydrolase, 1,3-1,4-beta-D-glucan-4-glucano hydrolase, 1,3-1,4-beta-D-glucanase, 1,3-1,4-beta-glucanase, 1,3;1,4-beta-glucan 4-glucanohydrolase, 1,3;1,4-beta-glucan endohydrolase, Af-EGL7, Afu6g01800, Beg1, beta-(1,3-1,4)-glucanase, beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase, beta-1,3-1,4 glucanase, beta-1,3-1,4-D-glucanase, beta-1,3-1,4-glucanase, beta-1,3;1,4-glucanase, beta-1-3, 1-4 glucan 4-glucanohydrolase, beta-glucanase, BG1, Bg1314, Bga1, bgc, bgi, Bgl, bgl5-1, BglA, BglA13, BglA16, BglA51, BglBB, bglBC1, BGlc8H, BglM2, BglS, BglT, BglTO, Bglu16A, bifunctional xylanase/endoglucanase, BLB369, BLB369 endo-beta-1,3-1,4-glucanase, Blc8H, BP_Cel9A, Cel5F, CP7 beta-1,3-1,4-glucanase, CtGlu16A, Cthe_0211, CtLic16A, CtLic26A, E-LICHN, EG1, EGL, EII, endo-(1,3)(1,4)-beta-glucanase, endo-(1,3;1,4)-beta-glucanase, endo-beta-1,3-1,4 glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3;1,4-glucan-D-glycosyl hydrolase, endo-beta-glucanase, endoglucanase, endotype beta-1,3-1,4-glucanase, Fisuc_2961, Fsbeta-glucanase, FSU_0226, Gcs2, GH7 endo-1,4-beta-glucanase, GHF16 TFsbeta-glucanase, GHF17 barley 1,3-1,4-beta-D-glucanase, Glc16A, GLU-1, GLU-3, glu369, Gluc5_26A, GluIII, GluUS570, glycoside hydrolase family 9 endoglucanase, GyrA, H(A16-M), lam1, LamA, laminarinase, Lic16A, Lic8H, LicA, LicB, Lichenase, lichenase-2, LicKM, licM, LicMB, LicS, McLic1, mHG, Mixed linkage beta-glucanase, More, NFEg16A, PbBglu16A, PlicA, PtLic16A, Ra0505, RuCelA, TaGlu34, TC2, TC5, TF-glu, TF-glucanase, theme C glycoside hydrolase family 9 endo-beta-glucanase, TM1752, US8_01508, XynIII, XynZ, ZgLamA

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.73 licheninase

Crystallization

Crystallization on EC 3.2.1.73 - licheninase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
1.5 A resolution, native enzyme, 1.6 A resolution, enzyme-inhibitor Glc-beta-1,3-isofagomine-complex, hanging drop vapor diffusion method for the enzyme, sitting drop vapor diffusion method for the complex
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crystal structure to 1.95 A resolution. The enzyme folds into a classic GH16 beta-jellyroll architecture which consists of two beta-sheets atop each other, with the substrate-binding cleft lying on the concave side of the inner beta-sheet. Two Bis–Tris propane molecules are in the positive and negative substrate binding sites
purified recombinant catalytic domain, sitting drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 25 mM Tris pH 7.5, 150 mM NaCl, and 0.002 ml reservori solution containing 0.04 M citric acid, 0.06 M Bis-Tris propane, pH 6.4, 18% w/v PEG 3350, 25°C, 7 days, optimized method, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method
molecular modeling of structures of wild-type and mutant K142N/Q203L/N214D does not reveal obvious differences in structure
molecular modeling of structure. Residues T2, S5,Y7, N14, S44, N78, S143, Y144, T146, D161, Q163, W209 and K213 are implicated in the contact between two monomers
enzyme-substrate complex, experiments by car-Parinello molecular dynamics simulations combined with force field molecular dynamics QM/MM CPMD, substrate 4-methylumbelliferyl tetrasaccharide
-
H(A16-M) in complex with beta-glucan tetrasaccharide, resolution range from 34.5 A to 1.64 A, hanging-drop vapour diffusion, room temperature
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homology modeling of structure. The enzyme is primarily composed of a beta-sheet, with two juxtaposed curved antiparallel beta-sheets consisting of seven strands. It forms a single compact globular domain, creating a deep cavity as a carbohydrate-binding channel for beta-glucan. The carbohydrate-binding region is a type B domain
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homology modeling of structure. Amino acid residues expected to form hydrogen bond with beta-glucan, nucleophile Glu134, the acid/base catalyst Glu138, Tyr152 and water mediate hydrogen bonds with Asn55, Gln148, Asn150, Glu160, and Asn211, are found in the active site cleft
the crystal structure of the enzyme is used for structure modelling, PDB ID 3O5S
molecular dynamic simulation and and optimization of residue sites in the calcium region to increase the thermostability
-
apo-form and substrate complex structures of mutant V18Y/W203Y, to 1.53 A resolution
mutant E85I, at 2.2 A resolution, by hanging-drop vapour-diffusion method at room temperature. The mutant crystallizes in space group P3121 with one molecule in the asymmetric unit, Ca2+ ion-binding site is maintained
mutant F40I, to 1.7 A resolution. Overall globular structures in the wild-type and mutant F40I enzymes do not differ
mutant W203F of truncated beta-glucanase catalytic domain, residues 1-243, to 1.4 A resolution. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202
purified recombinant mutant V18Y/W203Y alone and in complex with product cellotetraose , from 0.1 M Tris–HCl, pH 7.5, 0.3 M calcium acetate, and 29% PEG 5000 MME for the free mutant, and 0.15 M Tris, pH 8.5, 0.4 M calcium acetate and 33% PEG 5000 MME plus soaking in mother liquor with 5 mM cellotetraose for 1 h for the complexed mutant, X-ray diffraction structure determination and analysis at 1.53 A resolution, molecular replacement method
truncated form of enzyme containing the catalytic domain from amino acid 1-258, seleno-methionine labeled protein
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purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit
hanging drop vapor diffusion method, using 7.5% (v/v) 2-methyl-2,4-pentanediol, 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, and 0.1 M Tris (base)/Bicine, pH 8.5
to 1.8 A resolution
the structure of Gluc5_26A adopts a stable trimeric quaternary structure also observable in solution. The N-terminal region protrudes into the active site of an adjacent monomer. The N-terminus governs the substrate specificity of Gluc5_26A. Its deletion opens the enzyme cleft at the -3 subsite and turns the enzyme into an endo-beta(1,4)-glucanase
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