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Literature summary for 2.3.3.16 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)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

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

pH Optimum

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