Literature summary for 1.1.3.2 extracted from

Aki, K.; Yorita, K.; Massey, V.
Thermodynamic properties of L-lactate oxidase reconstituted with modified flavins (2000), Biofactors, 11, 115-116 .

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Organism

Organism	UniProt	Comment	Textmining
Aerococcus viridans	Q44467	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	redox potential difference is a dominant factor in determing rate of reduction. The enzyme reconstituted with a series of flavins modified at 6 or 8 position of the isoalloxazine ring shows a close linear relationship between reduction rate constant and redox potential in the ranges of -250 mV to -100 mV when L-lactate is used as substrate. The reconstituted enzyme shows a close linear relationship in the ranges of -150 mV to +100 mV when L-mandelate is used as substrate	Aerococcus viridans	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FMN	The standard redox potentials of enzyme-FMN/enzyme-FMNH and enzyme-FMNH/enzyme-FMNH2 are -95 mV and -161 mV, respectively, at pH 7.0, 25°C in 0.01 M imidazol buffer	Aerococcus viridans

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Release 2023.1 (January 2023)