Literature summary for 1.13.12.4 extracted from

Muh, U.; Williams, C.H., Jr.; Massey, V.
Lactate monooxygenase. II. Site-directed mutagenesis of the postulated active site base histidine 290 (1994), J. Biol. Chem., 269, 7989-7993.

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Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzyme H290Q expressed in Escherichia coli	Mycolicibacterium smegmatis

Protein Variants

Protein Variants	Comment	Organism
H290Q	the ability of L-lactate to reduce the enzyme flavin is abolished, whereas reoxidation of reduced enzyme with oxygen proceeds at a rate like that found in the wild type enzyme. Unlike the situation with wild type enzyme, where the transition state analog oxalate is bound tightly in a two-step reaction involving proton uptake from solution, the mutant enzyme binds oxalate weakly, in a single step reaction. Replacing the histidine has a significant effect on the ability of the enzyme to stabilize the flavin N(5)-sulfite adduct. Sulfite is bound at least 1000fold weaker than it is in the wild type enzyme	Mycolicibacterium smegmatis

Inhibitors

Inhibitors	Comment	Organism	Structure
D-lactate	competitive	Mycolicibacterium smegmatis

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium smegmatis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-lactate + O2	-	Mycolicibacterium smegmatis	acetate + CO2 + H2O	-	?

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Release 2023.1 (January 2023)