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Kinetics and Mechanism
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Catalytic Residues
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Three-dimensional structures
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Family Firsts
First stereochemistry determination
1,2-α-L-Fucosidase from Bifidobacterium bifidum, determined by 1H-NMR using 2'-fucosyllactose as a substrate.[5].
First molecular cloning
1,2-α-L-Fucosidase from Bifidobacterium bifidum, by expression cloning using a genomic library conctructed in Escherichia coli.[5].
First catalytic base identification
1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis and chemical rescue of the mutants [6].
First catalytic acid residue identification
1,2-α-L-Fucosidase from Bifidobacterium bifidum, kinetic analysis of the mutant [6].
First 3-D structure
The catalytic domain of 1,2-α-L-fucosidase from Bifidobacterium bifidum,wild-type enzyme in apo-form, E566A in complex with 2'-fucosyllactose, D766A in complex with fucose and lactose [6].
