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Information on EC 2.3.3.16 - citrate synthase (unknown stereospecificity) and Organism(s) Acetobacter aceti and UniProt Accession P20901

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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:
Acetobacter aceti
UNIPROT: P20901
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Word Map
The taxonomic range for the selected organisms is: Acetobacter aceti
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, bifunctional citrate synthase/2-methylcitrate synthase, citrate condensing enzyme, citrate synthase cit1, 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
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-, -, -, -, -, -, -, -, -, -, -, -, -
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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
hexameric type II citrate synthase
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CISY_ACEAC
436
0
48197
Swiss-Prot
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with oxaloacetate and inhibitor carboxymethyldethia-coenzyme A. The surface of citrate synthase is decoreated abundantly with basic side chains and this constellation is stable in varied pH environments
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Francois, J.A.; Starks, C.M.; Sivanuntakorn, S.; Jiang, H.; Ransome, A.E.; Nam, J.W.; Constantine, C.Z.; Kappock, T.J.
Structure of a NADH-insensitive hexameric citrate synthase that resists acid inactivation
Biochemistry
45
13487-13499
2006
Acetobacter aceti (P20901), Acetobacter aceti
Manually annotated by BRENDA team