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Literature summary for 3.2.1.51 extracted from

  • Kovalova, T.; Koval, T.; Benesova, E.; Vodickova, P.; Spiwok, V.; Lipovova, P.; Dohnalek, J.
    Active site complementation and hexameric arrangement in the GH family 29; a structure-function study of alpha-L-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus (2019), Glycobiology, 29, 59-73 .
    View publication on PubMed
Search for more literature for 3.2.1.51

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Paenibacillus thiaminolyticus

Protein Variants

Protein Variants Comment Organism
W392A the oligomeric state of the protein is not changed by the mutation. The mutant enzyme is used in crystallization experiments, but it does not produce any crystals. For 4-nitrophenyl-alpha-L-fucoside, the mutation causes an increase in KM, while the maximal rate changed only slightly. When 2'-fucosyllactose is hydrolyzed, KM for the mutant-catalyzed reaction stays about the same, while the maximal rate decreases three times compared to the wild type. The mutation negatively affects the rate of reaction, which results in lower yields. It has no effect on the type of substrate the enzyme can deglycosylate. The mutation does not affect the ability of the enzyme to transfer L-fucose to a specific type of the acceptor molecule Paenibacillus thiaminolyticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
 4-nitrophenyl-alpha-L-fucoside wild-type enzyme, pH 8, 45°C Paenibacillus thiaminolyticus
5.8
-
 4-nitrophenyl-alpha-L-fucoside mutant enzyme W392A, pH 8, 45°C Paenibacillus thiaminolyticus
19
-
 2'-fucosyllactose mutant enzyme W392A, pH 8, 45°C Paenibacillus thiaminolyticus
20
-
 2'-fucosyllactose wild-type enzyme, pH 8, 45°C Paenibacillus thiaminolyticus

Organism

Organism UniProt Comment Textmining
Paenibacillus thiaminolyticus E3PQQ9
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
190
-
 substrate: 4-nitrophenyl-alpha-L-fucoside, mutant enzyme W392A, pH 8, 45°C Paenibacillus thiaminolyticus
275
-
 substrate: 4-nitrophenyl-alpha-L-fucoside, wild-type enzyme, pH 8, 45°C Paenibacillus thiaminolyticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-fucosyllactose + H2O
-
 Paenibacillus thiaminolyticus alpha-L-fucose + lactose
-
 ?
4-nitrophenyl-alpha-L-fucoside + H2O
-
 Paenibacillus thiaminolyticus 4-nitrophenol + alpha-L-fucose
-
 ?
additional information the enzyme is capable of transglycosylation on a variety of acceptor molecules, including saccharides, alcohols or chromogenic substrates Paenibacillus thiaminolyticus ?
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Paenibacillus thiaminolyticus

Synonyms

Synonyms Comment Organism
alpha-L-fucosidase isoenzyme 1
-
 Paenibacillus thiaminolyticus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
59
-
 melting temperature of wild-type enzyme Paenibacillus thiaminolyticus
60
-
 melting temperature of mutant enzyme W392A Paenibacillus thiaminolyticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5 mutant enzyme W392A Paenibacillus thiaminolyticus
8.5
-
 wild-type enzyme Paenibacillus thiaminolyticus