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Literature summary extracted from

  • Arnott, M.A.; Michael, R.A.; Thompson, C.R.; Hough, D.W.; Danson, M.J.
    Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic archaea, Thermoplasma acidophilum and Pyrococcus furiosus (2000), J. Mol. Biol., 304, 657-668.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.3.16 expression of chimeric mutant in Escherichia coli citrate synthase deficient strain MOB154 Thermoplasma acidophilum
2.3.3.16 expression of wild-type, chimeric mutant and site-directed mutants in Escherichia coli citrate synthase deficient strain MOB154 Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.3.16 crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus Pyrococcus furiosus
2.3.3.16 crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus Thermoplasma acidophilum

Protein Variants

EC Number Protein Variants Comment Organism
2.3.3.16 D113A site-directed mutagenesis, deletion of C-terminal amino acid residues which arrange the subunit contact, slightly increased Km for acetyl-CoA and oxaloacetate, slightly increased reaction velocity, reduced thermostability Pyrococcus furiosus
2.3.3.16 D113S site-directed mutagenesis, deletion of C-terminal amino acid residues which arrange the subunit contact, slightly decreased Km for acetyl-CoA and oxaloacetate, slightly increased reaction velocity, reduced thermostability Pyrococcus furiosus
2.3.3.16 additional information construction of mutant with disrupted inter-subunit ionic network by partly eleminating the C-terminal end amino acid residues, increased Km for substrates, reduced thermostability Pyrococcus furiosus
2.3.3.16 additional information construction of chimeric enzyme mutants with mix of the large and small subunits of Thermoplasma acidophilum and Pyrococcus furiosus, functional analysis of the subunits Pyrococcus furiosus
2.3.3.16 additional information construction of chimeric enzyme mutants with mix of the large and small subunits of Thermoplasma acidophilum and Pyrococcus furiosus, functional analysis of the subunits Thermoplasma acidophilum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.3.16 0.002
-
 oxaloacetate wild-type Thermoplasma acidophilum
2.3.3.16 0.004
-
 acetyl-CoA wild-type Pyrococcus furiosus
2.3.3.16 0.005
-
 acetyl-CoA wild-type Thermoplasma acidophilum
2.3.3.16 0.015
-
 oxaloacetate wild-type Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
2.3.3.16 Pyrococcus furiosus
-
-
-
2.3.3.16 Thermoplasma acidophilum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.3.16 recombinant chimeric mutants from E. coli Thermoplasma acidophilum
2.3.3.16 recombinant wild-type, chimeric mutants, C-terminal deletion mutants, and D113 mutants from E. coli Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.3.16 acetyl-CoA + oxaloacetate + H2O
-
 Pyrococcus furiosus citrate + CoA
-
 ?
2.3.3.16 acetyl-CoA + oxaloacetate + H2O
-
 Thermoplasma acidophilum citrate + CoA
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.3.16 dimer
-
 Pyrococcus furiosus
2.3.3.16 dimer
-
 Thermoplasma acidophilum
2.3.3.16 More chimeric mutants with exchanged large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus, the large subunit is responsible for subunit interaction, the small subunit is responsable for catalytic activity Pyrococcus furiosus
2.3.3.16 More chimeric mutants with exchanged large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus, the large subunit is responsible for subunit interaction, the small subunit is responsable for catalytic activity Thermoplasma acidophilum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.3.16 65
-
 enzyme mutant lacking 13 amino acid residues of the C-terminal Pyrococcus furiosus
2.3.3.16 65 70 chimeric mutant containing the large subunit of Pyrcoccus furiosus and the small subunit of Thermoplasma acidophilum Pyrococcus furiosus
2.3.3.16 65 70 chimeric mutant containing the large subunit of Pyrcoccus furiosus and the small subunit of Thermoplasma acidophilum Thermoplasma acidophilum
2.3.3.16 70 75 wild-type Thermoplasma acidophilum
2.3.3.16 75
-
 enzyme mutant lacking 2 amino acid residues of the C-terminal Pyrococcus furiosus
2.3.3.16 80
-
 mutants D113S and D113A Pyrococcus furiosus
2.3.3.16 90
-
 above, wild-type Pyrococcus furiosus
2.3.3.16 90
-
 chimeric mutant containing the large subunit of Thermoplasma acidophilum and the small subunit of Pyrcoccus furiosus Pyrococcus furiosus
2.3.3.16 90
-
 chimeric mutant containing the large subunit of Thermoplasma acidophilum and the small subunit of Pyrcoccus furiosus Thermoplasma acidophilum

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.3.16 40 90
-
 Pyrococcus furiosus
2.3.3.16 40 90
-
 Thermoplasma acidophilum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.3.16 additional information
-
 thermostability of wild-type and chimeric mutants Pyrococcus furiosus
2.3.3.16 additional information
-
 thermostability of wild-type and chimeric mutants Thermoplasma acidophilum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.3.16 8
-
 enzyme assay at Pyrococcus furiosus
2.3.3.16 8
-
 enzyme assay at Thermoplasma acidophilum