Literature summary extracted from

Ghisla, S.; Ogata, H.; Massey, V.; Schonbrunn, A.; Abeles, R.H.; Walsh, C.T.
Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate] 2-hydroxy-3-butynoate (1976), Biochemistry, 15, 1791-1797.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.13.12.4	2-Hydroxy-3-butynoate	irreversible inactivator due to a covalent modification of the bound FMN	Mycolicibacterium smegmatis

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.13.12.4	1.41	-	DL-2-hydroxy-3-butynoate	-	Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.13.12.4	(S)-lactate + O2	Mycolicibacterium smegmatis	-	acetate + CO2 + H2O	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.13.12.4	Mycolicibacterium smegmatis	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.13.12.4	(S)-lactate + O2	-	Mycolicibacterium smegmatis	acetate + CO2 + H2O	-	?
1.13.12.4	2-hydroxy-3-butynoate + O2	-	Mycolicibacterium smegmatis	?	-	?
1.13.12.4	DL-2-hydroxy-3-butynoate + O2	-	Mycolicibacterium smegmatis	?	-	?

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Release 2023.1 (January 2023)