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Literature summary for 3.2.1.38 extracted from

  • Parikh, M.R.; Matsumura, I.
    Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase (2005), J. Mol. Biol., 352, 621-628.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.38

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase, random mutagenesis of beta-galactosidase active site residues D201, H540, and N604, and high-throughput screening, the mutants show increased kcat/KM in beta-fucosidase reaction, and decreased activity in beta-galactosidase reaction, overview Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.56
-
 4-nitrophenyl-beta-D-fucopyranoside 25°C, recombinant mutant H540V/N604T of beta-galactosidase, EC 3.2.1.22 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-fucopyranoside + H2O recombinant mutant H540V/N604T of beta-galactosidase, EC 3.2.1.22 Escherichia coli 4-nitrophenol + beta-D-fucose
-
 ?

Synonyms

Synonyms Comment Organism
beta-fucosidase
-
 Escherichia coli
More cf. EC 3.2.1.22, beta-galactosidase Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21.5
-
 4-nitrophenyl-beta-D-fucopyranoside 25°C, recombinant mutant H540V/N604T of beta-galactosidase, EC 3.2.1.22 Escherichia coli