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Literature summary extracted from

  • Kean, K.M.; Karplus, P.A.
    Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis (2019), Protein Sci., 28, 135-149 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.13.12.4 crystallized at 4°C in hanging drops with a reservoir solution of 0.1 M sodium citrate pH 4.6, 0.4 M lithium sulfate, and 0.4 M ammonium sulfate. Structures of Mycobacterium smegmatis wild-type enzyme and a wild-type-like C203A variant at 2.1 A and 1.7 A resolution, respectively 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 P21795
-
-

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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.4 lactate monooxygenase
-
 Mycolicibacterium smegmatis
1.13.12.4 LMO
-
 Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.4 FMN FMN-dependent enzyme Mycolicibacterium smegmatis