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3.2.1.24: alpha-mannosidase

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

Word Map on EC 3.2.1.24

Reaction

2-O-alpha-D-mannopyranosyl-D-mannopyranose
+
H2O
= 2 alpha-D-mannopyranose

Synonyms

1,2-alpha-D-mannosidase, 1,2-alpha-mannosidase, acid alpha-mannosidase, acidic alpha-mannosidase, alpha 1,2-mannosidase, Alpha mannosidase 6A8B, alpha-1,2-mannosidase, alpha-1,3 mannosidase, alpha-1,4 mannosidase, alpha-D-mannopyranosidase, alpha-D-mannosidase, Alpha-D-mannoside mannohydrolase, alpha-man, alpha-mann, alpha-mannosidase, alpha-mannosidase C, alpha-mannosidase E-II, alpha-mannosidase I, alpha-mannosidase IA, alpha-mannosidase II, alpha-mannosidase III, alpha1,2-mannosidase, AMAN, class II alpha-mannosidase, CpGH125, ER-alpha-mannosidase, ER-mannosidase II, exo-alpha-mannosidase, GH38 alpha-mannosidase, GH38 alpha-mannosidase II, GH38 class II alpha-mannosidase, GH38 enzyme, Golgi alpha-mannosidase II, Golgi mannosidase IA, Golgi mannosidase IB, Laman, Lysosomal acid alpha-mannosidase, lysosomal alpha-D-mannosidase, lysosomal alpha-mannosidase, Man1p, MAN2B1, Man2C1, Man2C1 alpha-mannosidase, ManA, mannanase, MGG_00994.6, More, neutral alpha-mannosidase, neutral/cytosol mannosidase, p-nitrophenyl-alpha-mannosidase, SpGH125, SpGH38, Ssa-man, SSO3006, TM1851, TMM, velmanase alfa

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.24 alpha-mannosidase

Crystallization

Crystallization on EC 3.2.1.24 - alpha-mannosidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.7 A resolution
X-ray crystal structures obtained in apo-, inhibitor-bound, and substrate-bound forms provide both mechanistic and molecular insight into how the proteins, which adopts an (alpha/alpha)6fold, recognizes and hydrolyzes the alpha1,6-mannosidic bond by an inverting, metal-independent catalytic mechanism
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hanging drop vapour diffusion method, crystallization of wild-type enzyme in complex with 5-fluoro-beta-L-gulosyl fluoride, mutant enzyme D341N in complex with 2-deoxy-2-fluoro-alpgha-D-mannosyl fluoride and mutant enzyme D341N in complex with 5-fluoro-beta-L-gulosyl fluoride
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in complex with inhibitors mannoimidazole, glucoimidazole, N-octyl-6-epi-valienamine, gluco-hydroxyiminolactam, and [[(3S,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)piperidin-2-ylidene]amino] N-(4-chlorophenyl)carbamate
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vapor diffusion and micro-batch crystallization techniques, crystal structure in absence and presence of the anti-cancer agent swainsonine and the inhibitor deoxymannojirimycin
Drosophila sp. (in: flies)
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structual 3D analysis
30 mg/ml purified recombinant Golgi alpha-mannosidase IA in 20 mM MES, pH 6.5, 150 mM NaCl, 5 mM CaCl2, and 0.75 M NDSB-201, crystallization of free enzyme by microbatch method using a precipitation solution containing 15-20% PEG 4000 at pH 4.5-6.5, cocrystallization of 1-deoxymannojirimycin bound to the enzyme by hanging drop vapour diffusion method at 37°C, 0.001 ml of a solution containing 200 mM 1-deoxymannojirimycin is mixed with an equal volume of crystallization solution containing 100 mM MES and 100 mM Tris-HCl, pH 6.0, and 25-35% PEG 4000, 2 days at 18°C, X-ray diffraction structure determination and analysis at 1.5 A resolution, structure modelling
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crystal structure at 2.8 A resolution
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purified recombinent enzyme free or in complex with the inhibitor swainsonine, sitting drop vapour diffusion method, mixing of 12 mg/ml protein in 100 mM Tris, pH 8.5, 1.5 M (NH4)2SO4 and 12% v/v glycerol, with reservoir solution, containing 3% v/v glycerol, 54% v/v Tacsimate, pH 7.0, and 2% v/v PEG 6000, also acting as the cryo-protectant, crystals of the swainsonine complex form are obtained by soaking SpGH38 crystals for ,16 h in mother liquor supplemented with 2 mM swainsonine, X-ray diffraction structure determination and analysis at 1.9 A and 2.6 A resolution, respectively
purified recombinant TM1851, sitting drop vapour diffusion method, optimal conditions: 0.001 ml of protein solution containing 5.3 mg/ml protein in 5 mM sodium phosphate and 150 mM NaCl, pH 6.8, mixed with an equal volume of reservoir solution containing 4% w/v PEG 6000, 50 mM sodium phosphate, pH 6.0, and 0.5 M NaCl, 1 day at 25°C, X-ray diffraction structure determination and preliminary analysis at 2.9 A resolution
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