3.2.1.63: 1,2-alpha-L-fucosidase

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For detailed information about 1,2-alpha-L-fucosidase, go to the full flat file.

Reaction

Synonyms

1,2-alpha-L-fucosidase, Afc3, AfcA, AfcA protein, alpha(1,2) fucosidase, alpha-(1--> 2)-L-fucosidase, alpha-fucosidase, alpha-L-fucosidase, alpha-L-fucosidase II, alpha1,2-FUC, alpha1,2-fucosidase, bfo_2737, FgFCO1, Fuc1, FucNaFLD, fucosidase, 1,2-alpha-L-, More

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.63 1,2-alpha-L-fucosidase

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Results	in table
4	Activating Compound
16	AA Sequence
3	Application
1	CAS Registry Number
10	Cloned(Commentary)
2	Crystallization (Commentary)
1	Expression
8	General Information
3	General Stability
13	IC50 Value
64	Inhibitors
1	kcat/KM [mM/s]
9	Ki Value [mM]
21	KM Value [mM]
3	Localization
4	Metals/Ions
7	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
27	Organism
7	PDB ID
7	pH Optimum
4	pH Range
4	pH Stability
1	pI Value
1	Posttranslational Modification
17	Protein Variants
11	Purification (Commentary)
4	Reaction
2	Reaction Type
27	Reference
3	Source Tissue
5	Specific Activity [micromol/min/mg]
74	Substrates and Products (Substrate)
10	Subunits
28	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
3	Temperature Range [°C]
8	Temperature Stability [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.63 - 1,2-alpha-L-fucosidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

of the AfcA catalytic domain in unliganded and complexed forms with the inhibitor deoxyfuconojirimycin, the substrate 2’-fucosyllactose, and the products L-fucose and lactose at 1.12-2.10 A resolution

Bifidobacterium bifidum

-

680783

purified deglycosylated recombinant enzyme in open or closed form or complexed with L-fucose, sitting-drop vapor diffusion method or batch method, several different crystal forms, mixing 0.001 ml of 14-16 mg/ml Endo H-treated fucosidase in 25 mM Tris, pH 7.5, with 0.001 ml of precipitant solution containing 0.1 M Tris, pH 8.0, and either 30% or 40% w/v PEG MME 2000, 20°C, 2-3 days, X-ray diffraction structure determination and analysis at 1.38-156 A resolution, molecular replacement method

Fusarium graminearum

J9UN47

732150