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Literature summary for 1.13.12.4 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

Protein Variants Comment Organism
H290Q
-
Mycolicibacterium smegmatis
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
R293K uncoupled reaction, no decarboxylation Mycolicibacterium smegmatis
Y152F nearly as active as wild-type Mycolicibacterium smegmatis
Y44F uncoupled reaction, no decarboxylation Mycolicibacterium smegmatis

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
-
-
-

Cofactor

Cofactor Comment Organism Structure
FMN
-
Mycolicibacterium smegmatis