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Literature summary for 1.13.12.4 extracted from

  • Ghisla, S.; Ogata, H.; Massey, V.; Schonbrunn, A.; Abeles, R.H.; Walsh, C.T.
    Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate] 2-hydroxy-3-butynoate (1976), Biochemistry, 15, 1791-1797.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-Hydroxy-3-butynoate irreversible inactivator due to a covalent modification of the bound FMN Mycolicibacterium smegmatis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.41
-
DL-2-hydroxy-3-butynoate
-
Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactate + O2 Mycolicibacterium smegmatis
-
acetate + CO2 + H2O
-
?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + O2
-
Mycolicibacterium smegmatis acetate + CO2 + H2O
-
?
2-hydroxy-3-butynoate + O2
-
Mycolicibacterium smegmatis ?
-
?
DL-2-hydroxy-3-butynoate + O2
-
Mycolicibacterium smegmatis ?
-
?