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Literature summary extracted from

  • Muh, U.; Williams, C.H., Jr.; Massey, V.
    Lactate monooxygenase. III. Additive contributions of active site residues to catalytic efficiency and stabilization of an anionic transition state (1994), J. Biol. Chem., 269, 7994-8000.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.13.12.4 H290Q
-
Mycolicibacterium smegmatis
1.13.12.4 K266M the rate of reduction with (S)-lactate is decreased compared with that of the wild-type enzyme, the mutant enzyme is virtually inactive Mycolicibacterium smegmatis
1.13.12.4 R293K uncoupled reaction, no decarboxylation Mycolicibacterium smegmatis
1.13.12.4 Y152F nearly as active as wild-type Mycolicibacterium smegmatis
1.13.12.4 Y44F uncoupled reaction, no decarboxylation Mycolicibacterium smegmatis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.12.4 0.44
-
(S)-lactate Y44F mutant Mycolicibacterium smegmatis
1.13.12.4 6
-
(S)-lactate Y152F mutant Mycolicibacterium smegmatis
1.13.12.4 10
-
(S)-lactate R293K mutant Mycolicibacterium smegmatis
1.13.12.4 20
-
(S)-lactate H290Q mutant Mycolicibacterium smegmatis
1.13.12.4 22
-
(S)-lactate wild-type Mycolicibacterium smegmatis

Organism

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.4 FMN
-
Mycolicibacterium smegmatis