3.2.1.111: 1,3-alpha-L-fucosidase

This is an abbreviated version!
For detailed information about 1,3-alpha-L-fucosidase, go to the full flat file.

Reaction

Synonyms

AfcB, almond emulsin fucosidase I, alpha(1,3/4)-transfucosidase, alpha-1,3/4-L-fucosidase, alpha-L-fucosidase I, alphafuc, BbAfcB, cFase I, core fucosidase I, CpAfc2, fucosidase, 1,3-alpha-L-

ECTree

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.111 1,3-alpha-L-fucosidase

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Results	in table
2	Activating Compound
9	AA Sequence
1	CAS Registry Number
5	Cloned(Commentary)
1	General Information
3	General Stability
11	Inhibitors
25	kcat/KM [mM/s]
26	KM Value [mM]
4	Metals/Ions
3	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
10	Organism
8	PDB ID
4	pH Optimum
3	pH Range
2	pH Stability
24	Protein Variants
8	Purification (Commentary)
1	Reaction
1	Reaction Type
10	Reference
3	Source Tissue
3	Specific Activity [micromol/min/mg]
3	Storage Stability
44	Substrates and Products (Substrate)
3	Subunits
18	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]
24	Turnover Number [1/s]

Engineering

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Engineering on EC 3.2.1.111 - 1,3-alpha-L-fucosidase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

F34H/L321P

Bifidobacterium longum subsp. infantis

B7GNN8

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

750709

F34I/L321P

Bifidobacterium longum subsp. infantis

B7GNN8

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

750709

F34Y/L321P

Bifidobacterium longum subsp. infantis

B7GNN8

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

750709

L321P

Bifidobacterium longum subsp. infantis

B7GNN8

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

750709

F34H/L321P

Bifidobacterium longum subsp. infantis ATCC 15697

-

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

-

F34I/L321P

Bifidobacterium longum subsp. infantis ATCC 15697

-

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

-

F34Y/L321P

Bifidobacterium longum subsp. infantis ATCC 15697

-

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

-

L321P

Bifidobacterium longum subsp. infantis ATCC 15697

-

the mutant exhibits increased transfucosylation activity compared to the wild type enzyme

-

249DELTA265

Elizabethkingia meningoseptica

-

the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (14fold) 3-fucosyllactose (5fold) and Lewis X trisaccharide (9fold) compared to the wild type enzyme

751107

C317A

Elizabethkingia meningoseptica

-

the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (9fold) 3-fucosyllactose (4fold) and Lewis X trisaccharide (6fold) compared to the wild type enzyme

751107

C317S

Elizabethkingia meningoseptica

-

the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (2fold) 3-fucosyllactose (3fold) and Lewis X trisaccharide (2fold) compared to the wild type enzyme

751107

C467S

Elizabethkingia meningoseptica

-

the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (0.9fold) 3-fucosyllactose (0.9fold) and Lewis X trisaccharide (9fold) compared to the wild type enzyme

751107

C73S

Elizabethkingia meningoseptica

-

the mutant shows wild type activity with 4-nitrophenyl alpha-L-fucoside and Lewis X trisaccharide and shows decreased activity with 3-fucosyllactose (2fold) compared to the wild type enzyme

751107

D242A

Elizabethkingia meningoseptica

-

the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (10000fold) and Lewis X trisaccharide (1928fold) compared to the wild type enzyme

751107

E302A

Elizabethkingia meningoseptica

-

the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (736fold) and Lewis X trisaccharide (900fold) compared to the wild type enzyme

751107

E315A

Elizabethkingia meningoseptica

-

the mutant is inactive with 4-nitrophenyl alpha-L-fucoside and shows decreased activity with 3-fucosyllactose (473fold) and Lewis X trisaccharide (585fold) compared to the wild type enzyme

751107

C317S

Elizabethkingia meningoseptica FMS-007

-

the mutant shows decreased activity with 4-nitrophenyl alpha-L-fucoside (2fold) 3-fucosyllactose (3fold) and Lewis X trisaccharide (2fold) compared to the wild type enzyme

-

C73S

Elizabethkingia meningoseptica FMS-007

-

the mutant shows wild type activity with 4-nitrophenyl alpha-L-fucoside and Lewis X trisaccharide and shows decreased activity with 3-fucosyllactose (2fold) compared to the wild type enzyme

-

D242A

Elizabethkingia meningoseptica FMS-007

-

the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (10000fold) and Lewis X trisaccharide (1928fold) compared to the wild type enzyme

-

E302A

Elizabethkingia meningoseptica FMS-007

-

the mutant is inactive with 3-fucosyllactose and shows decreased activity with 4-nitrophenyl alpha-L-fucoside (736fold) and Lewis X trisaccharide (900fold) compared to the wild type enzyme

-

E315A

Elizabethkingia meningoseptica FMS-007

-

the mutant is inactive with 4-nitrophenyl alpha-L-fucoside and shows decreased activity with 3-fucosyllactose (473fold) and Lewis X trisaccharide (585fold) compared to the wild type enzyme

-

additional information

5 entries

additional information

Bifidobacterium bifidum

-

introduction of afcB gene into the Bacterioides longum 105-A strain, which has no intrinsic alpha-L-fucosidase. The transformant is able to utilize 3-fucosyllactose and lacto-N-fucopentaose II as the sole carbon source

708607

additional information

Bifidobacterium bifidum

C5NS94

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%)

750434

additional information

Bifidobacterium bifidum

-

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%)

750434

additional information

Clostridium perfringens

A0A0H2YQI3

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%)

750434

additional information

Clostridium perfringens

-

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%)

750434