Literature summary for 2.3.3.16 extracted from

Sievers, M.; Stoeckli, M.; Teuber, M.
Purification and properties of citrate synthase from Acetobacter europaeus (1997), FEMS Microbiol. Lett., 146, 53-58.

Search for more literature for 2.3.3.16

Activating Compound

Activating Compound	Comment	Organism	Structure
acetate	-	Komagataeibacter europaeus

Inhibitors

Inhibitors	Comment	Organism	Structure
ATP	25% inhibition at 10 mM	Komagataeibacter europaeus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.02	-	oxaloacetate	-	Komagataeibacter europaeus
0.051	-	acetyl-CoA	-	Komagataeibacter europaeus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
additional information	-	N-terminal protein sequence	Komagataeibacter europaeus
46000	-	6 * 46000, SDS-PAGE, amino-terminal amino acid sequence	Komagataeibacter europaeus
280000	-	gel filtration	Komagataeibacter europaeus

Organism

Organism	UniProt	Comment	Textmining
Komagataeibacter europaeus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Komagataeibacter europaeus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
230	-	purified enzyme	Komagataeibacter europaeus

Storage Stability

Storage Stability	Organism
-20°C, potassium phosphate buffer, pH 7.2, 15% glycerol, several weeks	Komagataeibacter europaeus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + oxaloacetate + H2O	-	Komagataeibacter europaeus	citrate + CoA	-	?

Subunits

Subunits	Comment	Organism
hexamer	6 * 46000, SDS-PAGE, amino-terminal amino acid sequence	Komagataeibacter europaeus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.1	-	-	Komagataeibacter europaeus

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Release 2023.1 (January 2023)