2.3.3.16: citrate synthase (unknown stereospecificity)
This is an abbreviated version!
For detailed information about citrate synthase (unknown stereospecificity), go to the full flat file.
Word Map on EC 2.3.3.16
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2.3.3.16
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4.1.3.7
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malate
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1.1.1.35
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glyoxysomal
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1.2.4.1
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al-induced
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agriculture
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synthesis
- 2.3.3.16
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4.1.3.7
- malate
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1.1.1.35
- glyoxysomal
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1.2.4.1
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al-induced
- agriculture
- synthesis
Reaction
Synonyms
bifunctional citrate synthase/2-methylcitrate synthase, CCNA_01983, CIT1, CitA, citrate condensing enzyme, citrate oxaloacetate-lyase (CoA-acetylating), citrate oxaloacetate-lyase, CoA-acetylating, citrate synthase, citrate synthase Cit1, citrate synthase/2-methylcitrate synthase, citrate synthetase, citric synthase, citric-condensing enzyme, citrogenase, CitZ, CS, CS1, CS2, CS3, CS4, CSI, CSY, CSY4, CTS, EC 4.1.3.7, gltA, GltA2, MCS, mitochondrial citrate synthase, mmgD, More, Msed_1522, oxalacetic transacetase, oxaloacetate transacetase, peroxisomal citrate synthase, Rv0896, SbnG, Si-citrate synthase, sll0401, SSO2589, St0589, St1805, synthase, citrate, TTHA1343, type II citrate synthase
ECTree
2.3.3.16 citrate synthase (unknown stereospecificity)Advanced search results
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results (Inhibitors
Inhibitors on EC 2.3.3.16 - citrate synthase (unknown stereospecificity)
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
elongation factor 1alpha
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causes polymerization of 49K protein, reduced activity
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Guanidinium chloride
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irreversible inactivation of recombinant wild-type at 1.6 M and of recombinant mutant G196V at 0.2 M, at 0.5 M activation of the wild-type
p-hydroxymercuribenzoate
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60% inhibition at 0.1 mM, protection by oxaloacetate
S-carboxymethyl-CoA
competitive inhibition versus acetyl-CoA, non-competitive inhibition versus oxaloacetate; inhibits the native enzyme competitively versus acetyl-CoA and non-competitively versus oxaloacetate
Urea
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irreversible inactivation of recombinant wild-type at 9.3 M and of recombinant mutant G196V at 5 M, at up to 8 M activation of the wild-type
5,5'-dithiobis(2-nitrobenzoate)
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inactivation of the glyoxysomal isozyme, half-life: approx. 1 min, not mitochondrial isozyme
5,5'-dithiobis(2-nitrobenzoate)
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inactivation, half-lifes at 0.4 mM: 2.8 min for CS 1, 50 min for CS II
ADP
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CS II insensitive, CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
AMP
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CS II insensitive, CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
ATP
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50% inhibition at 5 mM, competitive against acetyl-CoA; feed back inhibition
ATP
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isoenzyme CSII, 30% activity at 1 mM, isoenzyme CSI not inhibited at 1 mM
ATP
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20%, 40%, and 60% inhibition at 1 mM, 2 mM, and 5 mM ATP, respectively
citrate
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competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
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competitive with acetyl-CoA, noncompetitive with oxaloacetate
citrate
product inhibition, competitive. Citrate binds tightly to the substrate binding site and its binding induces a compact closed conformation
CoA
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competitive with acetyl-CoA, noncompetitive with oxaloacetate
KCl
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CS I inhibited competitively with acetyl-CoA, noncompetitively with oxaloacetate
NADH
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inhibition of wild-type enzyme. Inhibition is extremenly weak in mutant enzymes Y145A, R163L, and K167A
NADH
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0.1 M, 92% inhibition of wild-type, 25% inhibition of K283 acetylated variant, 88% inhibition of K295 acetylated variant, 7% inhibition of K168 acetylated variant
NADH
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10 mM, 31% inhibition; 1-10 mM; non-specific, 31% inhibition at 10 mM
NADH
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78% inhibition by 0.1 mM of CS I, 15% inhibition of CS II at 1 mM; isoenzyme CSI 78% at 0.1 mM, allosteric, isoenzyme CSII 15% activity at 1 mM
NADH
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CS II inhibited, CS II insensitive; weak inhibition, reversible by AMP, hinders the activation by AMP, CS II
NADH
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51% inhibition of peroxisomal isozyme, 12% inhibition of mitochondrial isozyme at 5 mM
p-chloromercuribenzoate
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can be restored by dithiothreitol treatment
additional information
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the activity is not affected by O2, pCMB (0.05 mM), or EDTA (0.05 mM)
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additional information
allosteric inhibition mechanism, structure relationship
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additional information
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allosteric inhibition mechanism, structure relationship
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additional information
no inhibition by NADH or 2-oxaloacetate
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additional information
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low salt concentrations inactivate reversibly
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additional information
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isocitrate, (R)-3-hydroxybutyrate, malonate, pyruvate, acetoacetyl, NaCl, NH4Cl, CsCl, and RbCl have no effect
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additional information
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NADH and AMP not inhibitory for small isoenzyme
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additional information
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NADH and AMP not inhibitory for small isoenzyme
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additional information
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NADH and AMP not inhibitory for small isoenzyme
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additional information
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NADH and AMP not inhibitory for small isoenzyme
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additional information
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NADH and AMP not inhibitory for small isoenzyme
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additional information
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NADH and AMP not inhibitory for the small isoenzyme
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additional information
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NADH and AMP not inhibitory for small isoenzyme
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additional information
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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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additional information
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NADH and AMP are not inhibitory for isoenzyme small
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additional information
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inhibited by a specific antibody against 49K protein
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