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Information on EC 2.3.3.16 - citrate synthase (unknown stereospecificity) and Organism(s) Homo sapiens and UniProt Accession O75390

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EC Tree
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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This record set is specific for:
Homo sapiens
UNIPROT: O75390
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
citrate synthetase, mitochondrial citrate synthase, peroxisomal citrate synthase, si-citrate synthase, type ii citrate synthase, citrate synthase cit1, bifunctional citrate synthase/2-methylcitrate synthase, citrate condensing enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
citrate condensing enzyme
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citrate oxaloacetate-lyase (CoA-acetylating)
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citrate oxaloacetate-lyase, CoA-acetylating
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citrate synthase
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citrate synthetase
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citric synthase
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citric-condensing enzyme
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citrogenase
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oxalacetic transacetase
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oxaloacetate transacetase
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synthase, citrate
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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 hide
9027-96-7
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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
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-
?
NATURAL SUBSTRATE
NATURAL 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
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-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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enzymatic activities of citrate synthase and isocitrate dehydrogenase IDH2 are significantly reduced in methyl 4 phenylpyridinium treatment cells, while protein acetylation of citrate synthase and IDH2 increase. Overexpressed sirtuin SIRT3 partially reverses at least, the decline of citrate synthase activity and the increase of citrate synthase protein acetylation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CISY_HUMAN
466
0
51712
Swiss-Prot
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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SIRT3 deacetylates and activates citrate synhase activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roy, C.
Insight into sequence, structure and homology modelling of mitochondrial citrate synthase of Homo sapience
Int. J. Pharm. Bio Sci.
6
B1309-B1321
2015
Homo sapiens (O75390)
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Manually annotated by BRENDA team
Cui, X.X.; Li, X.; Dong, S.Y.; Guo, Y.J.; Liu, T.; Wu, Y.C.
SIRT3 deacetylated and increased citrate synthase activity in PD model
Biochem. Biophys. Res. Commun.
484
767-773
2017
Homo sapiens
Manually annotated by BRENDA team