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Literature summary extracted from

  • Molgat, G.F.; Donald, L.J.; Duckworth, H.W.
    Chimeric allosteric citrate synthases: construction and properties of citrate synthases containing domains from two different enzymes (1992), Arch. Biochem. Biophys., 298, 238-246.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.3.16 expression of a chimeric protein with one Acinetobacter domain in Escherichia coli, domain interactions, subunit interactions Escherichia coli
2.3.3.16 expression of a chimeric protein with one Escherichia coli domain in Escherichia coli, domain interactions, subunit interactions Acinetobacter calcoaceticus subsp. anitratus

Protein Variants

EC Number Protein Variants Comment Organism
2.3.3.16 additional information chimeric proteins Escherichia coli
2.3.3.16 additional information chimeric proteins Acinetobacter calcoaceticus subsp. anitratus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.3.16 NADH allosteric Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 NADH allosteric Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.16 0.011
-
 oxaloacetate wild-type Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 0.02
-
 oxaloacetate wild-type Escherichia coli
2.3.3.16 0.11
-
 acetyl-CoA wild-type Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 0.7
-
 acetyl-CoA wild-type Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.3.16 KCl mutants, overview Escherichia coli
2.3.3.16 KCl mutants, overview Acinetobacter calcoaceticus subsp. anitratus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.3.16 additional information
-
 alignment of partial amino acid sequence Escherichia coli
2.3.3.16 additional information
-
 alignment of partial amino acid sequence Acinetobacter calcoaceticus subsp. anitratus

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.16 Acinetobacter calcoaceticus subsp. anitratus
-
-
-
2.3.3.16 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.16 recombinant chimeric protein from E. coli Escherichia coli
2.3.3.16 recombinant chimeric protein from E. coli Acinetobacter calcoaceticus subsp. anitratus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.3.16 additional information
-
 influence of KCl on wild-type and mutants Escherichia coli
2.3.3.16 additional information
-
 influence of KCl on wild-type and mutants Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 45
-
 purified wild-type enzyme Escherichia coli
2.3.3.16 57
-
 purified recombinant chimeric Acinetobacter-type protein with small E. coli domain Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 88
-
 purified wild-type enzyme Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 120
-
 purified recombinant chimeric E. coli-type protein with small Acinetobacter domain Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.16 acetyl-CoA + oxaloacetate + H2O
-
 Escherichia coli citrate + CoA
-
 ?
2.3.3.16 acetyl-CoA + oxaloacetate + H2O
-
 Acinetobacter calcoaceticus subsp. anitratus citrate + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.3.16 More recombinant chimeric enzymes, domain functions, subunit organisation Escherichia coli
2.3.3.16 More recombinant chimeric enzymes, domain functions, subunit organisation Acinetobacter calcoaceticus subsp. anitratus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.3.16 additional information
-
 additional information chimeric mutants, overview Escherichia coli
2.3.3.16 additional information
-
 additional information chimeric mutants, overview Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 78
-
 acetyl-CoA wild-type, + 0.1 M KCl Acinetobacter calcoaceticus subsp. anitratus
2.3.3.16 81
-
 acetyl-CoA wild-type, + 0.1 M KCl Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.3.16 7.8
-
 recombinant chimeric protein Escherichia coli