Literature summary for 1.5.3.25 extracted from

Wu, X.; Palfey, B.A.; Mossine, V.V.; Monnier, V.M.
Kinetic studies, mechanism, and substrate specificity of amadoriase I from Aspergillus sp. (2001), Biochemistry, 40, 12886-12895 .

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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	-	?

General Information

General Information	Comment	Organism
metabolism	the active configuration of the substrate is the alpha-pyranose form. The reductive half-reaction is triphasic and is consistent either with the reaction of the substrate with the flavin followed by iminium deprotonation or hydrolysis and then product release or with the formation of flavin reduction intermediates (carbanion equivalents or adducts), followed by product release. In the oxidative half-reaction, the reduced flavin is oxidized by O2 in a single phase. The redox potentials of amadoriase at pH 7.0, 25°, show values of +48 and -52 mV for the oxidized enzyme/anionic semiquinone and anionic semiquinone/reduced enzyme couples, respectively	Aspergillus sp.

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Release 2023.1 (January 2023)