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Literature summary for 3.2.1.111 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
Search for more literature for 3.2.1.111

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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

Organism UniProt Comment Textmining
Bifidobacterium bifidum C5NS94
-
-
Clostridium perfringens A0A0H2YQI3
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bifidobacterium bifidum
-
 Clostridium perfringens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-fucosyllactose + H2O
-
 Bifidobacterium bifidum ?
-
 ?
3-fucosyllactose + H2O
-
 Clostridium perfringens D-fucose + D-Gal-beta-(1->4)-D-Glc
-
 ?
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 ?
-
 ?
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

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