Fructosyl-peptide Oxidase (FPOX-CET)

  • Enzymes for Clinical Chemistry

The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.

Origin recombinant E. coli
Systematic name

Fructosyl-peptide : oxygen oxidoreductase

EC Number 1.5.3
Reaction formula

Fructosyl-L-amino acid + H2O + O2 →→→ Peptide + Glucosone + H2O2

SPECIFICATION

Appearance yellow lyophilizate
Activity ≧5.0 U/mg lyophilizate
Stabilizer glutamate, EDTA
Storage below -20℃ protected from light

PROPERTIES

Molecular weight ca. 60 kDa (gel filtration)
Structure monomer of 52 kDa(SDS-PAGE)
Michaelis constant 1.5×10-3M(fructosyl-valyl-histidine)
5.0×10-3M (fructosyl-glysine)
9.0×10-3M(Nε-fructosyl-lysine)
pH Optimum 7.5–8.5
pH Stability 5.5–9.5
Optimum temperature 37–45℃
Thermal stability below 45℃
Stability (powder form) stable at -20℃ for at least 12 months
Inhibitors Hg2+ ,Pb2+
Specificity fructosyl-valyl-histidine (100), fructosyl-glycine(150)
Nε-fructosyl-L-lysine (68.6)

APPLICATIONS

The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.

REFERENCES

Hirokawa, K. et al., Biochem. Biophys. Res. Commun., 311, 104-111 (2003).

Hirokawa, K., Shimoji, K., & Kajiyama, N. (2005).
An enzymatic method for the determination of hemoglobinA1C.
Biotechnology letters, 27(14), 963-968.

Hirokawa, K., Ichiyanagi, A., & Kajiyama, N. (2008).
Enhancement of thermostability of fungal deglycating enzymes by directed evolution.
Applied microbiology and biotechnology, 78(5), 775-781.

Ichiyanagi, A., Hirokawa, K., Gomi, K., Nakatsu, T., Kato, H., & Kajiyama, N. (2013).
Crystallization and preliminary crystallographic analysis of two eukaryotic fructosyl peptide oxidases.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(2), 130-133.

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