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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.4 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

EC Number Inhibitors Comment Organism Structure
1.13.12.4 D-lactate competitive Mycolicibacterium smegmatis

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 L-lactate + O2
-
Mycolicibacterium smegmatis acetate + CO2 + H2O
-
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