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Literature summary for 3.2.1.63 extracted from

  • Liu, J.; Zheng, M.; Zhang, C.; Xu, D.
    Amide resonance in the catalysis of 1,2-alpha-L-fucosidase from Bifidobacterium bifidum (2013), J. Phys. Chem. B, 117, 10080-10092.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
N423G mutagenesis simulation, the mutant still has significant activity Bifidobacterium bifidum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2'-fucosyllactose + H2O Bifidobacterium bifidum
-
 L-fucose + lactose
-
 ?

Organism

Organism UniProt Comment Textmining
Bifidobacterium bifidum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(Glcalpha(1-4))n + H2O = (Glcalpha(1-4))n-4 + (Glcalpha(1-4))4 stepwise reaction mechanism, the first step is the proton transfer from N423 to D766, and the second step involves the hydrolysis reaction via the inversion mechanism catalyzed by the amide group of N423. Assisted by D766, N423 serves as the general base to activate the water molecule to attack the anomeric carbon center. E566 is the general acid to facilitate the cleavage of glycosidic bond between L-fucose and galactose units. The intrinsic resonance structure for the side chain amide group of the asparagine residue is the origin to the catalytic activity Bifidobacterium bifidum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-fucosyllactose + H2O
-
 Bifidobacterium bifidum L-fucose + lactose
-
 ?
2'-fucosyllactose + H2O simulation of the reaction by the combined quantum mechanical and molecular mechanical approach. Molecular dynamics simulations and free energy profiles support that the overall reaction is a stepwise mechanism Bifidobacterium bifidum L-fucose + lactose
-
 ?

General Information

General Information Comment Organism
evolution the enzyme belongs to the glycosyl hydrolase family 29, GH29, of retaining fucosidases Bifidobacterium bifidum
additional information the side chain amide group of the asparagine residue, N423, is proposed to act as the general base to activate this water nucleophile, with assistance provided by a nearby D766. In the crystal structure, the D766 is hydrogen bonds with the N423 Bifidobacterium bifidum