Information on EC 2.3.3.3 - citrate (Re)-synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.3.3
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RECOMMENDED NAME
GeneOntology No.
citrate (Re)-synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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-
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enolization
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-
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hydrolysis
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citric acid cycle
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SYSTEMATIC NAME
IUBMB Comments
acetyl-coA:oxaloacetate C-acetyltransferase [thioester-hydrolysing, (pro-R)-carboxymethyl-forming]
This enzyme is inactivated by oxygen and is found in some anaerobes. Its stereospecificity is opposite to that of EC 2.3.3.1, citrate (Si)-synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
9077-70-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Clostridium acidi-urici
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-
-
Manually annotated by BRENDA team
Dehalococcoides sp.
designated as EC 2.3.3.14 but does not have any homocitrate synthase activity
Q3ZW76
UniProt
Manually annotated by BRENDA team
designated as EC 2.3.3.14 but does not have any homocitrate synthase activity
Q3ZW76
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the pathway via Re-citrate synthase contributes 30 to 40% to glutamate biosynthesis in Syntrophus aciditrophicus
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-citryl-CoA + H2O
citrate + CoA
show the reaction diagram
Clostridium acidi-urici
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-
-
r
(R)-malyl-CoA + H2O
(R)-malate + CoA
show the reaction diagram
Clostridium acidi-urici
-
-
-
r
acetyl-CoA + H2O + oxaloacetate
(R)-citrate + CoA
show the reaction diagram
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
show the reaction diagram
additional information
?
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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 + H2O + oxaloacetate
(R)-citrate + CoA
show the reaction diagram
acetyl-CoA + H2O + oxaloacetate
citrate + CoA
show the reaction diagram
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-
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
the enzyme contains stoichiometric amounts of Ca2+ (0.9 Ca/73 kDa)
Mg2+
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Mg2+ has no effect at all on enzyme activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
4-chloromercuribenzoate
4-hydroxymercuribenzoate
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complete inhibition at 0.1 mM
5,5'-dithiobis-2-nitrobenzoate
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30% inhibition at 10 mM
aerobic conditions
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50% inactivation in 24 h by aerobic conditions
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Cd2+
Clostridium acidi-urici
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complete inactivation
citrate
H2O2
Clostridium acidi-urici
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-
Hg2+
Clostridium acidi-urici
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complete inactivation
iodoacetamide
Clostridium acidi-urici
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strong inhibition
L-lysine
Dehalococcoides sp.
Q3ZW76
about 80% residual activity at 0.5 mM
p-chloromercuribenzoate
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0.002 mM, inactivation
Zn2+
Clostridium acidi-urici
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above 0.02 mM, activation below
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
AMP
Dehalococcoides sp.
Q3ZW76
about 120% activity at 0.15 mM
glutathione
Clostridium acidi-urici
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reducing reagent is required for maximal activity
L-cysteine
Clostridium acidi-urici
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reducing reagent is required for maximal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
(R)-citryl-CoA
Clostridium acidi-urici
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0.02
(R)-malyl-CoA
Clostridium acidi-urici
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-
0.05 - 0.13
acetyl-CoA
0.04 - 0.085
oxaloacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.72
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purified enzyme, in the absence of Mn2+, at pH 8.0 and 22°C
1.2
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purified enzyme, in the presence of 0.2 mM Mn2+, at pH 8.0 and 22°C
5.5
Clostridium acidi-urici
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
Clostridium acidi-urici
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sharp decrease in activity above
8
Clostridium acidi-urici
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
Clostridium acidi-urici
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approx. 50% activity at pH 7.0
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
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x * 52100, calculated, x * 51000, SDS-PAGE
52100
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x * 52100, calculated from sequence; x * 52100, calculated, x * 51000, SDS-PAGE
65000
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4 * 65000, SDS-PAGE
71800
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4 * 71800, calculated from amino acid sequence
72891
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4 * 72891, electrospray-time of flight mass spectrometry
271000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 52100, calculated from sequence; x * 52100, calculated, x * 51000, SDS-PAGE
homotetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-80
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the oxically purified enzyme loses 20% of its activity after each cycle of freezing at -80°C and thawing
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
reducing reagents and anaerobic conditions are required for maximal activity
Clostridium acidi-urici
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488157
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, the oxically purified enzyme, 20% loss of activity after each cycle of freezing at -80°C and thawing
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refrigerator, 24 h, 10% loss of activity
Clostridium acidi-urici
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isoelectric precipitate, DEAE-cellulose, ammonium sulfate, DEAE-Sephadex, ammonium sulfate, gel filtration
Clostridium acidi-urici
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isoelectric precipitation, DEAE-cellulose, DEAE-Sephadex
Clostridium acidi-urici
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recombinant enzyme
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Strep tag affinity column chromatography
Dehalococcoides sp.
Q3ZW76
Strep-tactin column chromatography and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 CodonPlus (DE3)-GroEL cells
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expressed in Escherichia coli BL21(DE3) cells
Dehalococcoides sp.
Q3ZW76
expression in Escherichia coli
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme inhibited by EDTA can be reactivated by Mg2+, Mn2+, Co2+
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