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Literature summary for 6.2.1.16 extracted from

  • Aneja, P.; Dziak, R.; Cai, G.Q.; Charles, T.C.
    Identification of an acetoacetyl coenzyme A synthetase-dependent pathway for utilization of L-(+)-3-hydroxybutyrate in Sinorhizobium meliloti (2002), J. BACTERIOL., 184, 1571-1577.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Sinorhizobium meliloti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 acetoacetate pH 8.4 Sinorhizobium meliloti
20
-
 L-3-hydroxybutyrate pH 8.4 Sinorhizobium meliloti

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
-
 Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by a method that includes His affinity resin chromatography Sinorhizobium meliloti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + acetoacetate + CoA
-
 Sinorhizobium meliloti AMP + diphosphate + acetoacetyl-CoA
-
 ?
ATP + L-3-hydroxybutyrate + CoA
-
 Sinorhizobium meliloti AMP + diphosphate + L-3-hydroxybutyryl-CoA
-
 ?