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Literature summary for 2.4.1.4 extracted from

  • van der Veen, B.A.; Skov, L.K.; Potocki-Veronese, G.; Gajhede, M.; Monsan, P.; Remaud-Simeon, M.
    Increased amylosucrase activity and specificity, and identification of regions important for activity, specificity and stability through molecular evolution (2006), FEBS J., 273, 673-681.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E227G mutant enzyme is a highly efficient polymerase that produces a longer polymer than the wild-type enzyme. Decreased stability and the temperature optimum compared to wild-type enzyme Neisseria polysaccharea
N387D 60% increase in activity compared to wild-type enzyme, increased stability at 50°C Neisseria polysaccharea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information
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Neisseria polysaccharea

Organism

Organism UniProt Comment Textmining
Neisseria polysaccharea Q9ZEU2
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Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
mutant enzyme E227G Neisseria polysaccharea
40
-
mutant enzyme N387D Neisseria polysaccharea
42
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wild-type enzyme Neisseria polysaccharea

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
rapid denaturation of wild-type enzyme Neisseria polysaccharea

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
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additional information
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Neisseria polysaccharea