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Information on EC 2.3.3.16 - citrate synthase (unknown stereospecificity) and Organism(s) Pyrococcus furiosus and UniProt Accession Q53554
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2.3.3.16 citrate synthase (unknown stereospecificity)IUBMB Comments
This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C-2 of oxaloacetate has not been established [cf. EC 2.3.3.1, citrate (Si)-synthase and EC 2.3.3.3, citrate (Re)-synthase].
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The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
citrate synthetase, mitochondrial citrate synthase, peroxisomal citrate synthase, si-citrate synthase, type ii citrate synthase, citrate condensing enzyme, citrate synthase cit1, bifunctional citrate synthase/2-methylcitrate synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
citrate condensing enzyme
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-
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citrate oxaloacetate-lyase (CoA-acetylating)
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-
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citrate oxaloacetate-lyase, CoA-acetylating
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-
-
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citrate synthase
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-
-
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citrate synthetase
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-
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citric synthase
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-
-
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citric-condensing enzyme
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-
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citrogenase
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-
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oxalacetic transacetase
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-
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oxaloacetate transacetase
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-
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synthase, citrate
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:oxaloacetate C-acetyltransferase (thioester-hydrolysing)
This entry has been included to accommodate those citrate synthases for which the stereospecificity with respect to C-2 of oxaloacetate has not been established [cf. EC 2.3.3.1, citrate (Si)-synthase and EC 2.3.3.3, citrate (Re)-synthase].
CAS REGISTRY NUMBER
COMMENTARY
9027-96-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65 - 70
-
chimeric mutant containing the large subunit of Pyrcoccus furiosus and the small subunit of Thermoplasma acidophilum
90
90
-
chimeric mutant containing the large subunit of Thermoplasma acidophilum and the small subunit of Pyrcoccus furiosus
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
dimer
additional information
additional information
subunit organisation from crystal structure, dimer
additional information
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, room temperature, 2 mg/ml protein concentration, precipitation by 0.1 M sodium citrate and 0.1 M ammonium phosphate, 20 mM Tris-HCl, pH 8.0, 25 mM KCl, x-ray structure analysis, structural basis of high thermostability
crystal structure analysis of chimeric mutants with exchange of large and small subunits between Thermoplasma acidophilum and Pyrococcus furiosus
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D113A
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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
D113S
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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
additional information
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
thermostability of wild-type and chimeric mutants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type, chimeric mutants, C-terminal deletion mutants, and D113 mutants from E. coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type, chimeric mutant and site-directed mutants in Escherichia coli citrate synthase deficient strain MOB154
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overexpression in Escherichia coli JM105, DNA and amino acid sequence analysis
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
complete recovery of activity is observed after incubation for 1 h at 50°C by a 20fold dilution in 50 mM phosphate buffer of the enzyme fully unfolded in 6 M guanidine-HCl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Russell, R.J.M.; Ferguson, J.M.C.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Angstroem resolution
Biochemistry
36
9983-9994
1997
Pyrococcus furiosus (Q53554)
Muir, J.M.; Russell, R.J.M.; Hough, D.W.; Danson, M.J.
Citrate synthase from the hyperthermophilic archaeon, Pyrococcus furiosus
Protein Eng.
8
583-592
1995
Pyrococcus furiosus
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
J. Mol. Biol.
304
657-668
2000
Pyrococcus furiosus, Thermoplasma acidophilum
Gerike, U.; Danson, M.J.; Hough, D.W.
Cold-active citrate synthase: mutagenesis of active-site residues
Protein Eng.
14
655-661
2001
Arthrobacter sp., Arthrobacter sp. DS2-3R, Pyrococcus furiosus
Moore, V.; Kanu, A.; Byron, O.; Campbell, G.; Danson, M.J.; Hough, D.W.; Crennell, S.J.
Contribution of inter-subunit interactions to the thermostability of Pyrococcus furiosus citrate synthase
Extremophiles
15
327-336
2011
Pyrococcus furiosus (Q53554)
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