Any feedback?
Information on EC 2.3.3.16 - citrate synthase (unknown stereospecificity) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00890
for references in articles please use BRENDA:EC2.3.3.16Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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].
Specify your search results
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
CIT1
citrate condensing enzyme
-
-
-
-
citrate oxaloacetate-lyase (CoA-acetylating)
-
-
-
-
citrate oxaloacetate-lyase, CoA-acetylating
-
-
-
-
citrate synthase
-
-
-
-
citrate synthetase
-
-
-
-
citric synthase
-
-
-
-
citric-condensing enzyme
-
-
-
-
citrogenase
-
-
-
-
oxalacetic transacetase
-
-
-
-
oxaloacetate transacetase
-
-
-
-
synthase, citrate
-
-
-
-
additional information
-
enzyme participates in multienzyme complexes of enzymes belonging to tricarboxylic acid cycle, probably substrate channeling, in vivo NMR measurements
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
free diffusion mechanism, no channeling of oxaloacetate from malate dehydrogenase
-
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
-
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 + oxaloacetate + H2O
citrate + CoA
-
no channeling of oxaloacetate between malate dehydrogenase and citrate synthase in a recombinant fusion protein using a coupled assay
-
ir
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
regulation of mitochondrial uptake and efflux by citrate synthase activity
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
?
additional information
?
-
no activity with propionyl-CoA
-
-
?
additional information
?
-
-
cells with cit1 deletion show higher tendency toward glutathione depletion and subsequent accumulation of reactive oxygen species than the wild type. GSH deficiency in cit1 null cells is caused by an insufficient supply of glutamate necessary for biosynthesis of GSH rather than the depletion of reducing power required for reduction of GSSG to GSH
-
-
?
additional information
?
-
-
yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase or aconitase share several growth phenotypes as well as patterns of specific protein expression that differ from the parental strain. These shared properties of idhD and aco1D strains are eliminated or moderated by codisruption of the CIT1 gene encoding mitochondrial citrate synthase
-
-
?
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
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
regulation of mitochondrial uptake and efflux by citrate synthase activity
-
-
?
acetyl-CoA + oxaloacetate + H2O
citrate + CoA
-
entry step to tricarboxylic acid cycle
-
?
additional information
?
-
-
cells with cit1 deletion show higher tendency toward glutathione depletion and subsequent accumulation of reactive oxygen species than the wild type. GSH deficiency in cit1 null cells is caused by an insufficient supply of glutamate necessary for biosynthesis of GSH rather than the depletion of reducing power required for reduction of GSSG to GSH
-
-
?
additional information
?
-
-
yeast mutants lacking mitochondrial NAD+-specific isocitrate dehydrogenase or aconitase share several growth phenotypes as well as patterns of specific protein expression that differ from the parental strain. These shared properties of idhD and aco1D strains are eliminated or moderated by codisruption of the CIT1 gene encoding mitochondrial citrate synthase
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
51% inhibition of peroxisomal isozyme, 12% inhibition of mitochondrial isozyme at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006 - 0.007
oxaloacetate
-
native and recombinant peroxisomal isozyme CS II
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
213
-
purified fusion protein of citrate synthase and mitochondrial malate dehydrogenase, coupled assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
45% of CS II is bound to mitochondrial inner membrane and 2% of CS I
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
additional information
-
enzyme participates in multienzyme complexes of enzymes belonging to tricarbonic acid cycle, probably substrate channeling, in vivo NMR measurements
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no channeling of oxaloacetate between malate dehydrogenase and citrate synthase in a recombinant fusion protein using a coupled assay
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged fusion protein of citrate synthase and mitochondrial malate dehydrogenase from E. coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of His-tagged fusion protein of citrate synthase and mitochondrial malate dehydrogenase, expression in Escherichia coli
-
expression of labeled mitochondrial isozyme in Saccharomyces from plasmid, NMR measurements in vivo
-
functional expression of peroxisomal isozyme CS II in citrate synthase deficient Escherichia coli mutant and wild-type Escherichia coli strain
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sandor, A.; Johnson, J.H.; Srere, P.A.
Cooperation between enzyme and transporter in the inner mitochondrial membrane of yeast
J. Biol. Chem.
269
29609-29612
1994
Saccharomyces cerevisiae
Kispal, G.; Srere, P.A.
Studies on yeast peroxisomal citrate synthase
Arch. Biochem. Biophys.
286
132-137
1991
Saccharomyces cerevisiae
Haggie, P.M.; Brindle, K.M.
Mitochondrial citrate synthase is immobilized in vivo
J. Biol. Chem.
274
3941-3945
1999
Saccharomyces cerevisiae
Pettersson, H.; Olsson, P.; Bulow, L.; Pettersson, G.
Kinetics of the coupled reaction catalyzed by a fusion protein of yeast mitochondrial malate dehydrogenase and citrate synthase
Eur. J. Biochem.
267
5041-5046
2000
Saccharomyces cerevisiae
Ruprich-Robert, G.; Zickler, D.; Berteaux-Lecellier, V.; Velot, C.; Picard, M.
Lack of mitochondrial citrate synthase discloses a new meiotic checkpoint in a strict aerobe
EMBO J.
21
6440-6451
2002
Saccharomyces cerevisiae, Podospora anserina (Q9HFI1), Podospora anserina
Graybill, E.R.; Rouhier, M.F.; Kirby, C.E.; Hawes, J.W.
Functional comparison of citrate synthase isoforms from S. cerevisiae
Arch. Biochem. Biophys.
465
26-37
2007
Saccharomyces cerevisiae (P00890)
Lin, A.P.; Hakala, K.W.; Weintraub, S.T.; McAlister-Henn, L.
Suppression of metabolic defects of yeast isocitrate dehydrogenase and aconitase mutants by loss of citrate synthase
Arch. Biochem. Biophys.
474
205-212
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
EXTERNAL LINKS (specific for EC-Number 2.3.3.16)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
