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Literature summary extracted from

  • Zeuner, B.; Vuillemin, M.; Holck, J.; Muschiol, J.; Meyer, A.S.
    Loop engineering of an alpha-1,3/4-L-fucosidase for improved synthesis of human milk oligosaccharides (2018), Enzyme Microb. Technol., 115, 37-44 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.111 expressed in Escherichia coli BL21 (DE3) Bifidobacterium bifidum
3.2.1.111 expressed in Escherichia coli BL21 (DE3) Clostridium perfringens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.111 additional information replacement of a 23 amino acids long alpha-helical loop close to the active site of alpha-1,3/4-L-fucosidase from Bifidobacterium bifidum with the corresponding 17-amino acid alpha-helical loop of alpha-1,3/4-L-fucosidase from Clostridium perfringens results in almost complete abolishment of the hydrolytic activity on 3-fucosyllactose (6000 times lower hydrolytic activity than wild-type enzyme from Bifidobacterium bifidum), while the transfucosylation activity is lowered one order of magnitude. The loop engineering results in an alpha-1,3/4-L-fucosidase with transfucosylation activity reaching molar yields of lacto-N-fucopentaose II of 39% on 3-fucosyllactose and negligible product hydrolysis. This is almost 3times higher than the yield obtained with wild-type enzyme from Bifidobacterium bifidum (14%) and comparable to that obtained with alpha-1,3/4-L-fucosidase from Clostridium perfringens (50%) Bifidobacterium bifidum
3.2.1.111 additional information replacement of a 23 amino acids long alpha-helical loop close to the active site of alpha-1,3/4-L-fucosidase from Bifidobacterium bifidum with the corresponding 17-amino acid alpha-helical loop of alpha-1,3/4-L-fucosidase from Clostridium perfringens results in almost complete abolishment of the hydrolytic activity on 3-fucosyllactose (6000 times lower hydrolytic activity than wild-type enzyme from Bifidobacterium bifidum), while the transfucosylation activity is lowered one order of magnitude. The loop engineering results in an alpha-1,3/4-L-fucosidase with transfucosylation activity reaching molar yields of lacto-N-fucopentaose II of 39% on 3-fucosyllactose and negligible product hydrolysis. This is almost 3times higher than the yield obtained with wild-type enzyme from Bifidobacterium bifidum (14%) and comparable to that obtained with alpha-1,3/4-L-fucosidase from Clostridium perfringens (50%) Clostridium perfringens

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.111 Bifidobacterium bifidum C5NS94
-
-
3.2.1.111 Clostridium perfringens A0A0H2YQI3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.111
-
 Bifidobacterium bifidum
3.2.1.111
-
 Clostridium perfringens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.111 3-fucosyllactose + H2O
-
 Bifidobacterium bifidum ?
-
 ?
3.2.1.111 3-fucosyllactose + H2O
-
 Clostridium perfringens D-fucose + D-Gal-beta-(1->4)-D-Glc
-
 ?
3.2.1.111 additional information the enzyme can catalyse formation of the human milk oligosaccharide lacto-N-fucopentaose II through regioselective transfucosylation of lacto-N-tetraose with 3-fucosyllactose as donor substrate Bifidobacterium bifidum ?
-
 ?
3.2.1.111 additional information the enzyme can catalyse formation of the human milk oligosaccharide lacto-N-fucopentaose II through regioselective transfucosylation of lacto-N-tetraose with 3-fucosyllactose as donor substrate Clostridium perfringens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.111 alpha-1,3/4-L-fucosidase
-
 Bifidobacterium bifidum
3.2.1.111 alpha-1,3/4-L-fucosidase
-
 Clostridium perfringens
3.2.1.111 BbAfcB
-
 Bifidobacterium bifidum
3.2.1.111 CpAfc2
-
 Clostridium perfringens