Crystallization (Comment) | Organism |
---|---|
homology modeling and docking of substrates fructosyl L-valine and Nepsilon-fructosyl-L-lysine. Residue Asn354 interacts closely with Nepsilon-fructosyl-L-lysine, but not with fructosyl L-valine | Pichia sp. N1-1 |
Protein Variants | Comment | Organism |
---|---|---|
N354A | mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine | Pichia sp. N1-1 |
N354H | mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine | Pichia sp. N1-1 |
N354K | mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine | Pichia sp. N1-1 |
N354V | mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine | Pichia sp. N1-1 |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.89 | - |
fructosyl L-valine | mutant N354H, pH 7, 25°C | Pichia sp. N1-1 | |
3 | - |
fructosyl L-valine | mutant N354A, pH 7, 25°C | Pichia sp. N1-1 | |
3.9 | - |
fructosyl L-valine | mutant N354K, pH 7, 25°C | Pichia sp. N1-1 | |
5.6 | - |
fructosyl L-valine | wild-type, pH 7, 25°C | Pichia sp. N1-1 | |
9.8 | - |
Nepsilon-fructosyl-L-lysine | wild-type, pH 7, 25°C | Pichia sp. N1-1 | |
10 | - |
fructosyl L-valine | mutant N354V, pH 7, 25°C | Pichia sp. N1-1 | |
63 | - |
Nepsilon-fructosyl-L-lysine | mutant N354A, pH 7, 25°C | Pichia sp. N1-1 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pichia sp. N1-1 | Q3L8U0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
fructosyl L-valine + O2 + H2O | poor substrate of isoform amadoriases I | Pichia sp. N1-1 | glucosone + L-valine + H2O2 | - |
? | |
Nepsilon-fructosyl-L-lysine + O2 + H2O | poor substrate of isoform amadoriases I | Pichia sp. N1-1 | glucosone + L-lysine + H2O2 | - |
? |