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Literature summary for 1.5.3.25 extracted from

  • Wu, X.; Takahashi, M.; Chen, S.G.; Monnier, V.M.
    Cloning of amadoriase I isoenzyme from Aspergillus sp. evidence of FAD covalently linked to Cys342 (2000), Biochemistry, 39, 1515-1521 .
    View publication on PubMed
Search for more literature for 1.5.3.25

Protein Variants

Protein Variants Comment Organism
C342A about 2% of wild-type activity, loss of covalent binding of FAD Aspergillus sp.
C342S less than 1% of wild-type activity, loss of covalnet binding of FAD Aspergillus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 fructosyl propylamine wild-type, pH 7.4, 37°C Aspergillus sp.
0.28
-
 fructosyl propylamine mutant C342S, pH 7.4, 37°C Aspergillus sp.
0.36
-
 fructosyl propylamine mutant C342A, pH 7.4, 37°C Aspergillus sp.

Organism

Organism UniProt Comment Textmining
Aspergillus sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fructosyl propylamine + O2 + H2O
-
 Aspergillus sp. glucosone + propylamine + H2O2
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.08
-
 fructosyl propylamine mutant C342S, pH 7.4, 37°C Aspergillus sp.
0.27
-
 fructosyl propylamine mutant C342A, pH 7.4, 37°C Aspergillus sp.
1.97
-
 fructosyl propylamine wild-type, pH 7.4, 37°C Aspergillus sp.

Cofactor

Cofactor Comment Organism Structure
FAD enzyme contains 1 mol of FAD per mol. FAD is covalently linked to Cys342 Aspergillus sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.28
-
 fructosyl propylamine mutant C342S, pH 7.4, 37°C Aspergillus sp.
0.73
-
 fructosyl propylamine mutant C342A, pH 7.4, 37°C Aspergillus sp.
40
-
 fructosyl propylamine wild-type, pH 7.4, 37°C Aspergillus sp.