Information on EC 2.3.3.1 - citrate (Si)-synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.3.3.1
-
RECOMMENDED NAME
GeneOntology No.
citrate (Si)-synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
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Citrate cycle (TCA cycle)
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citric acid cycle
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ethylene biosynthesis V (engineered)
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Glyoxylate and dicarboxylate metabolism
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glyoxylate cycle
-
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itaconate biosynthesis
-
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L-glutamine biosynthesis III
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Metabolic pathways
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methylaspartate cycle
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Microbial metabolism in diverse environments
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mixed acid fermentation
-
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partial TCA cycle (obligate autotrophs)
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-
TCA cycle I (prokaryotic)
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-
TCA cycle II (plants and fungi)
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TCA cycle III (animals)
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TCA cycle IV (2-oxoglutarate decarboxylase)
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TCA cycle V (2-oxoglutarate:ferredoxin oxidoreductase)
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TCA cycle VII (acetate-producers)
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TCA cycle VIII (helicobacter)
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-S)-carboxymethyl forming]
The stereospecificity of this enzyme is opposite to that of EC 2.3.3.3, citrate (Re)-synthase, which is found in some anaerobes. Citrate synthase for which the stereospecificity with respect to C2 of oxaloacetate has not been established are included in EC 2.3.3.16, citrate synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-96-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strain ATCC 14123
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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citrate synthase activity reduction leads to a strong L-lysine accumulation
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
show the reaction diagram
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no activation by metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
no inhibition
amphetamine
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valproate reverses and lithium prevents the enzyme inhibition
D-serine
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Ouabain
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activity was inhibited immediately after the administration of ouabain in the prefrontal cortex at the doses of 0.01 mM and 0.1 mM
SDS
-
strong inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
aldosterone
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 10
acetyl-CoA
0.0059 - 5
oxaloacetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.275 - 167
oxaloacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.076
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citrate synthase deficient strain
24
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purified enzyme
108
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purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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enzyme assay at
7.9
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enzyme assay at
8
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enzyme assay at
additional information
-
pI: 5.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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enzyme assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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highest at 4-cell stage
Manually annotated by BRENDA team
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left free wall shows higher activity than that at the apex
Manually annotated by BRENDA team
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cancer and normal tissue
Manually annotated by BRENDA team
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activity of citrate synthase is significantly higher compared with adjacent nonneoplastic tissue
Manually annotated by BRENDA team
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of female rats. Deep region closest have the highest citrate synthase activity
Manually annotated by BRENDA team
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trained and untrained
Manually annotated by BRENDA team
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a significant increase in maximal activity (63%) and expression (80%) of citrate synthase is observed in stimulated soleus muscles, isolated 1 h after electrical stimulation as compared to controls
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio vulnificus (strain CMCP6)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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gel filtration
104000
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gel filtration
250000
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gel filtration
additional information
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amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 47000, SDS-PAGE
tetramer
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2 * 45000 + 2 * 80000, alpha, beta, SDS-PAGE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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488052
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
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thermal inactivation: less than 12% of activity remains after 60 min
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
commercial preparation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA cloning and sequencing, mRNA expression pattern during embryonic development, DNA and amino acid sequence analysis
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EGFP-fusion version expressed in HeLa cell
expressed in Hep-G2 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
acute administration of olanzapine inhibits citrate synthase activity in cerebellum and prefrontal cortex
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Al3+ increases the expression level of citrate synthase gene and enzyme activity
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AlCl3 treatment
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during sexual development, the expression of citrate synthase is quite strong in cleistothecial shells. Acetate shows a strong inductive effect on citA expression, which is subjected to carbon catabolite repression caused by glucose
during sexual development, the expression of citrate synthase is significantly weak in the content of cleistothecia including ascospores
expression is regulated by catabolite control protein C (CcpC)
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in AlCl3 containing growth edium
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oanzapine 3 mg/kg and fluoxetine 12.5 mg/kg in combination increase citrate synthase activity in prefrontal cortex, hippocampus and striatum. The chronic administration of olanzapine increases citrate synthase activity in prefrontal cortex, hippocampus and striatum and fluoxetine increases citrate synthase activity in striatum
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overexpression of retinoic acid receptor-related orphan receptor alpha (5fold), leads to a 94% increase in citrate synthase mRNA levels and enzyme activity in Hep-G2 cells
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the mRNA expression of citrate synthase in liver is reduced by 42% in the staggerer mice (which possess a nonfunctional retinoic acid receptor-related orphan receptor alpha protein) relative to the wild type mice
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H320G
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effect of H320G substitution, solvent accessibility, and conformational changes on catalysis and activity
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
only after removal of 6 M denaturing guanidinium chloride by dialysis, not by dilution, dithiothreitol-dependent
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study on the mechanism of aggregation during refolding of enzyme and its prevention using cosolvent additives of the polyol series. No parallel correlation between the folding effect and the general stabilization is observed. Glycerol is most effective in enhancing the refolding yield of citrate synthase, and a complete recovery of enzymatic activity is observed at 7 M glycerol and 0.01 mg per ml protein. Kinetic experiments suggest that polyols act very early in the refolding process. Both the thermodynamic and the kinetic aspects are critical in the folding process
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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cellular stress marker
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