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]

Posttranslational Modification

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Posttranslational Modification on EC 3.2.1.63 - 1,2-alpha-L-fucosidase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

Fusarium graminearum

J9UN47

prediction of three N-glycosylation sites on Asn187, Asn280, and Asn401 (residues numbered for the protein without signal peptide). Deglycosylation of the recombinant enzyme expressed from Pichia pastoris by treatment with Endo H or peptide N-glycosidase F. The N-glycans on Asn-280 of the TIM barrel domain retained a chitobiose core and high mannose type substitutions, GlcNAc-beta1-4GlcNAc-beta1-4(Man-alpha1-6)Man-alpha1-3Man-alpha1-2Man-alpha1-2Man, possibly protected from EndoH by the beta,gamma-crystallin domain. The other two N-glycosylation sites Asn187 and Asn401 are each attached to one GlcNAc residue, indicative of Endo H cleavage. No effect of Endo H deglycosylation on the catalytic efficiency with small fucosylated substrates or on thermal stability, but higher solubility of the glycosylated than the deglycosylated enzyme

732150