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Literature summary for 1.5.3.25 extracted from

  • Miura, S.; Ferri, S.; Tsugawa, W.; Kim, S.; Sode, K.
    Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis (2006), Biotechnol. Lett., 28, 1895-1900 .
    View publication on PubMed
Search for more literature for 1.5.3.25

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pichia sp. N1-1

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of structure. Asn354 plays an important role in substrate recognition and can be substituted in order to change substrate specificity while maintaining high catalytic activity Pichia sp. N1-1

Protein Variants

Protein Variants Comment Organism
C324A mutation of putative active site residue, no residual activity with fructosyl L-valine Pichia sp. N1-1
F356A mutation of putative active site residue, 18% of wild-type activity with fructosyl L-valine Pichia sp. N1-1
K357A mutation of putative active site residue, 2% of wild-type activity with fructosyl L-valine Pichia sp. N1-1
K48A mutation of putative active site residue, no residual activity with fructosyl L-valine Pichia sp. N1-1
N354A substitution has no effect on the Vmax/Km value for fructosyl valine, but the Vmax/Km1 value for fructosyl-epsilonN-lysine is decreased 3fold Pichia sp. N1-1
N44A mutation of putative active site residue, 4% of wild-type activity with fructosyl L-valine Pichia sp. N1-1
N47A mutation of putative active site residue, 10% of wild-type activity with fructosyl L-valine Pichia sp. N1-1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8
-
 fructosyl L-valine mutant N47A, pH 7, 25°C Pichia sp. N1-1
3
-
 fructosyl L-valine mutant N354A, pH 7, 25°C Pichia sp. N1-1
5.4
-
 fructosyl L-valine mutant F356A, pH 7, 25°C Pichia sp. N1-1
5.4
-
 fructosyl L-valine mutant N44A, pH 7, 25°C Pichia sp. N1-1
5.6
-
 fructosyl L-valine wild-type, pH 7, 25°C Pichia sp. N1-1
10
-
 Nepsilon-fructosyl-L-lysine wild-type, pH 7, 25°C Pichia sp. N1-1
63
-
 Nepsilon-fructosyl-L-lysine mutant N354A, pH 7, 25°C Pichia sp. N1-1

Organism

Organism UniProt Comment Textmining
Pichia sp. N1-1 Q3L8U0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fructosyl L-valine + O2 + H2O
-
 Pichia sp. N1-1 glucosone + L-valine + H2O2
-
 ?
Nepsilon-fructosyl-L-lysine + O2 + H2O
-
 Pichia sp. N1-1 glucosone + L-lysine + H2O2
-
 ?