1.5.3.25: fructosyl amine oxidase (glucosone-forming)
This is an abbreviated version!
For detailed information about fructosyl amine oxidase (glucosone-forming), go to the full flat file.
Reaction
Synonyms
AgaE-like protein, amadoriase, amadoriase I, amadoriase II, FaoA, FAOAo1, FAOAo2, FAOD, FAOD-Ao1, FAOD-Ao2, FAOX, FAOX-C, FAOX-II, FrlB, fructosyl amine:oxygen oxidoreductase, fructosyl amino acid oxidase, GAOA
ECTree
1.5.3.25 fructosyl amine oxidase (glucosone-forming)Advanced search results
results (
results (Engineering
Engineering on EC 1.5.3.25 - fructosyl amine oxidase (glucosone-forming)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
T60A/A188G/M244L/N257S/L261M
mutant with improved thermostability, stable at 45°C
D295C/K303C
mutation leads to increase in melting temperature, mutant shows hyperstabilization with residual activity up to 95°C
E71S
mutation in salt bridge between flexible regions, activity similar to wild-type
E75N/R108L7R114W/W208R/Q289R/T303S
8.78fold increase in the activity toward fructosyl-polylysine and also performs several fold better than the wild-type on real gravy stains at concentrations of 10-100 microg/ml
K53M
more than a million-fold decrease in flavin reduction, while only slowing the oxygen reaction by about 30fold
N52A
mutation results in significant loss in the catalytic ability to employ O2 as the electron acceptor, while having little effect on the dye-mediated dehydrogenase activity employing artificial electron acceptors instead of O2
N63D/K64Q/R112W/V113F/R114S
strong increase in activity with fructosyl adamantanamine and with fructosyl polylysine
R112Y/V113F/R114S
strong increase in activity with fructosyl adamantanamine
R112E
R112E/R114E
-
mutation in isoform II, kcat value is similar to the wild-type, while the Km of the mutant toward fructosyl glycine increases significantly
R114E
K373M
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
K373R
-
mutant has lost the activity on substrate fructosyl valine
K373T
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
K373V
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
K373W
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
K373M
Fusarium oxysporum f. sp. raphani NBRC 9972
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
-
K373R
Fusarium oxysporum f. sp. raphani NBRC 9972
-
mutant has lost the activity on substrate fructosyl valine
-
K373T
Fusarium oxysporum f. sp. raphani NBRC 9972
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
-
K373V
Fusarium oxysporum f. sp. raphani NBRC 9972
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
-
K373W
Fusarium oxysporum f. sp. raphani NBRC 9972
-
catalytic turnover for fructosyl valine greatly decreases, whereas that for Nepsilon-fructosyl-Nalpha-benzyloxycarbonyl-L-lysine does not
-
C324A
mutation of putative active site residue, no residual activity with fructosyl L-valine
F356A
mutation of putative active site residue, 18% of wild-type activity with fructosyl L-valine
K357A
mutation of putative active site residue, 2% of wild-type activity with fructosyl L-valine
K48A
mutation of putative active site residue, no residual activity with fructosyl L-valine
N354A
N354H
mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine
N354K
mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine
N354V
mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine
N44A
mutation of putative active site residue, 4% of wild-type activity with fructosyl L-valine
N47A
R94W
-
specificity of mutant enzyme toward fructosyl valine is 14fold that of the wild-type enzyme
R112E
-
mutation in isoform II to the corresponding residue of isoform I, leads to reversal of the enzymatic activities toward fructosylglycine and fructosylpropylamine
R112E
-
mutation in isoform II, kcat value is similar to the wild-type, while the Km of the mutant toward fructosyl glycine increases significantly
R114E
-
mutation in isoform II to the corresponding residue of isoform I, leads to reversal of the enzymatic activities toward fructosylglycine and fructosylpropylamine
R114E
-
mutation in isoform II, kcat value is similar to the wild-type, while the Km of the mutant toward fructosyl glycine increases significantly
N354A
mutation leads to an increase in the activity ratio fructosyl L-valine/Nepsilon-fructosyl-L-lysine
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
N47A
mutation of putative active site residue, 10% of wild-type activity with fructosyl L-valine
N47A
mutation results in significant loss in the catalytic ability to employ O2 as the electron acceptor, while having little effect on the dye-mediated dehydrogenase activity employing artificial electron acceptors instead of O2
