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3.2.1.78: mannan endo-1,4-beta-mannosidase

This is an abbreviated version!
For detailed information about mannan endo-1,4-beta-mannosidase, go to the full flat file.

Word Map on EC 3.2.1.78

Reaction

Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Manbeta(1-4)Man
+
H2O
=
Manbeta(1-4)Manbeta(1-4)Man
+
Manbeta(1-4)Man

Synonyms

(1,4)-beta-D-mannan mannanohydrolase, 1,4-beta-D-mannan mannanohydrolase, 1,4-beta-mannanase, beta-1,4-D-mannanase, beta-1,4-mannan 4-mannanohydrolase, beta-1,4-mannanase, beta-D-mannanase, Beta-mannanase, beta-mannanase B, CaMan, CelB, cold-adapted beta-mannanase, CsMan5, CtManf, Dtur_0671, em26a, endo-1,4-beta-D-mannanase, endo-1,4-beta-mannanase, endo-1,4-mannanase, endo-acting beta-1,4-mannanase, endo-beta 1,4-mannanase, endo-beta-(1,4)-mannanase, endo-beta-(1->4)-mannanase, endo-beta-1,4 mannanase, endo-beta-1,4,D-mannanase, endo-beta-1,4-D-mannanase, endo-beta-1,4-mannanase, endo-beta-1,4-mannase, endo-beta-D-1,4-mannanase, endo-beta-D-mannanase, endo-beta-mannanase, endo-mannanase, GH 134 beta-1,4-mannanase, GH134, GH5-CBM27, KMAN-3, LeMAN4, LeMAN4a, Man, MAN I, Man II, MAN-P, Man1, Man113A, Man134A, Man26A, Man26A-50K, Man26b, Man4A, Man5, Man5A, Man5C, man5D, Man5P1, Man5XZ3, Man5_8, Man7, ManA, ManA/HmA, ManB, ManB-1601, ManC, ManEM17, ManF, ManH, ManIII, mannan endo-1,4-beta-mannanase, mannan endo-1,4-beta-mannosidase, mannan endo-1.4-beta-D-mannosidase, mannanase, mannanase, endo-1,4-beta-, ManP, ManS2, MYCTH_99077, PoMan5A, Rman, TpMan, TrMan5A

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.78 mannan endo-1,4-beta-mannosidase

Crystallization

Crystallization on EC 3.2.1.78 - mannan endo-1,4-beta-mannosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and selenomethionyl enzyme, to 1.9 and 1.99 A resolution, respectively
-
to 1.45 A resolution, crystal shows a typical (beta/alpha)8 folding type. The catalytic acid/base Glu167 and nucleophile Glu266 are positioned on the beta4 and beta7 strands, respectively
hanging-drop vapor diffusion method at room temperature
-
enzyme in apoform and in complex with mannopentaose, the precipitant solution contains 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis, modelling
hanging drop vapor diffusion method, using 1 M ammonium citrate, 15% (v/v) isopropanol, and 0.1M Tris-HCl (pH 8.5)
both native protein and selenomethionyl derivative, enzyme expressed in Pichia pastoris
-
hanging drop vapour diffusion method, mixing of 6.5 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with reservoir solution containing 0.1 M magnesium chloride, 0.1 M sodium acetate pH 4.5, 23% w/v PEG 3350, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.40 A resolution, molecular replacement
hanging drop vapor diffusion
molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein
recombinant enzyme
-
homology modeling of structure
crystallization of catalytic domain. Crystals from conditions with phosphate or citrate salts as precipitant belong to space group P212121, resolution to 1.4 A, while a crystal from a condition with ethanol as precipitant belongs to space group I212121, resolution to 1.45 A
purified recombinant His-tagged full-length enzyme and catalytic domain, X-ray diffraction structure determination and analysis by dynamic light scattering and small-angle X-ray scattering. molecular modelling
purified recombinant isolated His-tagged catalytic domain in apoform and complexed with iodine, glucose, maltose, and maltose + gycerol, sitting drop vapor diffusion method, mixing of 0.0005 ml of 12 mg/ml protein in 25 mM Tris-HCl, pH 7.5, with 0.0005 ml of precipitant solution containing 0.1 M citrate, pH 5.5, 1 M ammonium phosphate, and 0.2 M sodium chloride, 20°C, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.40-1,92 A resolution