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Information on EC 2.3.3.16 - citrate synthase (unknown stereospecificity) and Organism(s) Saccharolobus solfataricus and UniProt Accession P80148
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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: Saccharolobus solfataricus
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, 
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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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-
-
-
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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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -
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
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
the activity with propanoyl-CoA is not tested
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
the activity with propanoyl-CoA is not tested
-
-
?
additional information
?
-
the activity with propanoyl-CoA is not tested
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-
?
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-carboxymethyl-CoA
competitive inhibition versus acetyl-CoA, non-competitive inhibition versus oxaloacetate
S-carboxymethyl-CoA
inhibits the native enzyme competitively versus acetyl-CoA and non-competitively versus oxaloacetate
additional information
-
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
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additional information
limited proteolysis of citrate synthase from Sulfolobus solfataricus by trypsin reduces the rate of the overall reaction (acetyl-CoA + oxaloacetate + H2O -> citrate + CoASH) to 4% but does not affect the hydrolysis of citryl-CoA. A connecting link between the enzyme's ligase and hydrolase activity becomes impaired specifically on treatment with trypsin. Other proteolytic enzymes like chymotrypsin and subtilisin inactivate catalytic functions of citrate synthase, ligase and hydrolase, equally well
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0075
acetyl-CoA
25°C, pH and temperature not specified in the publication
0.0183
oxaloacetate
25°C, pH and temperature not specified in the publication
0.0075
acetyl-CoA
pH and temperature not specified in the publication
0.0183
oxaloacetate
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
S-carboxymethyl-CoA
25°C, pH and temperature not specified in the publication, competitive inhibition versus acetyl-CoA
0.0024
S-carboxymethyl-CoA
25°C, pH and temperature not specified in the publication, non-competitive inhibition versus oxaloacetate
0.00037
S-carboxymethyl-CoA
pH and temperature not specified in the publication, competitively inhibition versus acetyl-CoA
0.0024
S-carboxymethyl-CoA
non-competitively inhibition versus oxaloacetate, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
isoelectric focusing, pH-range 5.5-8.5, 10°C, native citrate synthase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of rigidity in citrate synthases from thermophiles to investigate the relationship between rigidity and thermostability. The increase in rigidity does not detract from the functional flexibility of the active site in all systems once their respective temperature range has been reached. In hyperthermophiles, salt bridges have stabilising roles in the active site, occuring in close proximity to key residues involved in catalysis and binding of the protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
additional information
citrate synthase is converted by limited proteolysis into a citryl-CoA hydrolase. Tryptic hydrolysis occurs at the N-terminal region of citrate synthase. The peptide removed from the enzyme by trypsin contains less than about 15 amino acid residues
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 7-10 mg/ml, 50 mM Tris buffer, pH 8.0, stable for at least 1 year
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loehlein-Wehrhahn, G.; Goepfert, P.; Eggerer, H.
Purification and properties of an archaebacterial enzyme: citrate synthase from Sulfolobus solfataricus
Biol. Chem. Hoppe-Seyler
369
109-113
1988
Saccharolobus solfataricus
Bell, G.S.; Russell, R.J.; Connaris, H.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile
Eur. J. Biochem.
269
6250-6260
2002
Saccharolobus solfataricus (P80148), Saccharolobus solfataricus P2 (P80148)
Loehlein-Werhahn, G.; Goepfert, P.; Kollmann-Koch, A.; Eggerer, H.
Studies on the citryl-CoA-dependent inhibition of citrate-synthase with source variants from bakers yeast, Escherichia coli and Sulfolobus solfataricus
Biol. Chem. Hoppe-Seyler
369
417-424
1988
Saccharolobus solfataricus
Lill, U.; Lefrank, S.; Henschen, A.; Eggerer, H.
Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase
Eur. J. Biochem.
208
459-466
1992
Saccharolobus solfataricus, Saccharolobus solfataricus (P80148), Saccharolobus solfataricus P1, Saccharolobus solfataricus P2 (P80148)
Connaris, H.; West, S.M.; Hough, D.W.; Danson, M.J.
Cloning and overexpression in Escherichia coli of the gene encoding citrate synthase from the hyperthermophilic Archaeon Sulfolobus solfataricus
Extremophiles
2
61-66
1998
Saccharolobus solfataricus (P80148), Saccharolobus solfataricus P2 (P80148)
McManus, T.J.; Wells, S.A.; Walker, A.B.
Salt bridge impact on global rigidity and thermostability in thermophilic citrate synthase
Phys. Biol.
17
016002
2019
Thermoplasma acidophilum (P21553), Saccharolobus solfataricus (P80148), Thermus thermophilus (Q5SIM6), Thermus thermophilus DSM 579 (Q5SIM6), Saccharolobus solfataricus DSM 1617 (P80148)
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