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Literature summary for 5.4.99.1 extracted from

  • Roymoulik, I.; Moon, N.; Dunham, W.R.; Ballou, D.P.; Marsh, E.N.
    Rearrangement of L-2-hydroxyglutarate to L-threo-3-methylmalate catalyzed by adenosylcobalamin-dependent glutamate mutase (2000), Biochemistry, 39, 10340-10346.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2
-
L-2-hydroxyglutarate pH 7.0 Clostridium cochlearium

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-hydroxyglutarate rate-limiting step is most likely the rearrangement of the 2-hydroxyglutaryl radical to the 3-methylmalyl radical Clostridium cochlearium L-threo-3-methylmalate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
L-2-hydroxyglutarate pH 7.0 Clostridium cochlearium