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Literature summary for 3.2.1.18 extracted from

  • Watson, J.N.; Indurugalla, D.; Cheng, L.L.; Narine, A.A.; Bennet, A.J.
    The hydrolase and transferase activity of an inverting mutant sialidase using non-natural beta-sialoside substrates (2006), Biochemistry, 45, 13264-13275.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y370A catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 4% of the activity with Y370G Micromonospora viridifaciens
Y370G catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration Micromonospora viridifaciens
Y370N catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370N Micromonospora viridifaciens
Y370T catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370T Micromonospora viridifaciens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000023
-
phenyl beta-sialoside pH 5.25, 37°C, mutant enzyme Y370G Micromonospora viridifaciens
0.000045
-
phenyl alpha-sialoside pH 5.25, 37°C, mutant enzyme Y370G Micromonospora viridifaciens

Organism

Organism UniProt Comment Textmining
Micromonospora viridifaciens Q02834
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenyl alpha-sialoside + H2O
-
Micromonospora viridifaciens ?
-
?
phenyl beta-sialoside + H2O mutant enzymes Y370G, Y370A, Y370N and Y370T catalyze the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration. Mutant enzyme Y370A shows 4% of the activity of Y370G, mutant enzymes Y370N and Y370T show 9% of the activity of Y370G Micromonospora viridifaciens phenol + alpha-sialic acid
-
?
phenyl beta-sialoside + lactose the Y370G mutant can transfer the sialic acid moiety from phenyl beta-sialoside to lactose in yields of up to 13%13%. Greater than 90% of the sialyllactose product formed in the coupling reactions is the alpha-2,6-isomer. Micromonospora viridifaciens phenol + sialyllactose
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.82
-
phenyl alpha-sialoside pH 5.25, 37°C, mutant enzyme Y370G Micromonospora viridifaciens
13.3
-
phenyl beta-sialoside pH 5.25, 37°C, mutant enzyme Y370G Micromonospora viridifaciens