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Information on EC 2.3.3.1 - citrate (Si)-synthase and Organism(s) Sus scrofa and UniProt Accession P00889
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2.3.3.1 citrate (Si)-synthaseIUBMB Comments
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 C-2 of oxaloacetate has not been established are included in EC 2.3.3.16, citrate synthase (unknown stereospecificity).
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Word Map
- 2.3.3.1
- malate
- fiber
- succinate
-
endurance
- soleus
-
tricarboxylic
- cardiac
- lateralis
-
vastus
- gastrocnemius
- hexokinase
-
sedentary
- glycogen
-
treadmill
- isocitrate
-
phosphofructokinase
- creatine
- myosin
- carnitine
- rickettsia
-
krebs
- mtdna
- aconitase
-
untrained
- tick
- plantaris
- 3-hydroxyacyl-coa
-
bartonellae
-
vo2max
- quadriceps
-
fast-twitch
-
extensor
-
training-induced
-
submaximal
- fumarase
-
respirometry
-
slow-twitch
- tfam
-
ergometer
- ixodes
- pgc-1alpha
-
exercise-trained
-
sprint
-
shsps
-
capillarization
- flea
- anaplasma
- phagocytophilum
- ehrlichia
-
endurance-trained
- analysis
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
citrate synthase, citrate (si)-synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-citric synthase
-
-
-
-
citrate oxaloacetate-lyase ((pro-3S)-CH2COO---> acetyl-CoA)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -
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 C-2 of oxaloacetate has not been established are included in EC 2.3.3.16, citrate synthase (unknown stereospecificity).
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
-
intermediate citryl-CoA
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
encoded by nuclear DNA, precursor is synthesized in the cytosol, import into mitochondrion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CISY_PIG
464
0
51629
Swiss-Prot
Mitochondrion (Reliability: 2), Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
detection of peptides within the enzyme which show strong binding with small heat shock proteins. Thermostabilization of thermosensitive citrate synthase by small heat shock proteins is achieved by stabilization of the C- and N-terminae in the protruding thermosensitive softspot, which is absent in the thermostable forms of the enzymes dimer
additional information
detection of peptides within the enzyme which show strong binding with small heat shock proteins. Thermostabilization of thermosensitive citrate synthase by small heat shock proteins is achieved by stabilization of the C- and N-terminae in the protruding thermosensitive softspot, which is absent in the thermostable forms of the enzymes dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H320G
-
effect of H320G substitution, solvent accessibility, and conformational changes on catalysis and activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase
additional information
small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
only after removal of 6 M denaturing guanidinium chloride by dialysis, not by dilution, dithiothreitol-dependent
-
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kurz, L.C.; Shah, S.; Frieden, C.; Nakra, T.; Stein, R.E.; Drysdale, G.R.; Evans, C.T.; Srere, P.A.
Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site
Biochemistry
34
13278-13288
1995
Sus scrofa
Kelly, S.M.; Price, N.C.
Reactivation of denatured citrate synthase
Int. J. Biochem.
24
627-630
1992
Sus scrofa
Ahrman, E.; Gustavsson, N.; Hultschig, C.; Boelens, W.C.; Emanuelsson, C.S.
Small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase
Extremophiles
11
659-666
2007
Sus scrofa, Sus scrofa (P00889)
Mishra, R.; Seckler, R.; Bhat, R.
Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: how well are protein folding and stability aspects coupled?
J. Biol. Chem.
280
15553-15560
2005
Sus scrofa
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