acyltransferase, acyl groups converted into alkyl on transfer
citrate (Si)-synthase activity
RNA binding
Cellular component
mitochondrial matrix
extracellular exosome
mitochondrion
nucleus
Biological process
citrate metabolic process
tricarboxylic acid cycle
carbohydrate metabolic process
metabolism
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
1431
12974
Ensembl
ENSG00000062485
ENSMUSG00000005683
UniProt
O75390
Q9CZU6
RefSeq (mRNA)
NM_198324 NM_004077
NM_026444
RefSeq (protein)
NP_004068
NP_080720
Location (UCSC)
Chr 12: 56.27 – 56.3 Mb
Chr 10: 128.17 – 128.2 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Citrate synthase (E.C. 2.3.3.1 (previously 4.1.3.7)) is an enzyme that exists in nearly all living cells. It functions as a pace-making enzyme in the first step of the citric acid cycle (or Krebs cycle).[5] Citrate synthase is located within eukaryotic cells in the mitochondrial matrix, but is encoded by nuclear DNA rather than mitochondrial. It is synthesized using cytoplasmic ribosomes, then transported into the mitochondrial matrix.
Citrate synthase is commonly used as a quantitative enzyme marker for the presence of intact mitochondria. Maximal activity of citrate synthase indicates the mitochondrial content of skeletal muscle.[6] The maximal activity can be increased by endurance training or high-intensity interval training,[6] but maximal activity is further increased with high-intensity interval training.[7]
Citrate synthase catalyzes the condensation reaction of the two-carbon acetate residue from acetyl coenzyme A and a molecule of four-carbon oxaloacetate to form the six-carbon citrate:[5]
Oxaloacetate is regenerated after the completion of one round of the Krebs cycle.
Oxaloacetate is the first substrate to bind to the enzyme. This induces the enzyme to change its conformation, and creates a binding site for the acetyl-CoA. Only when this citryl-CoA has formed will another conformational change cause thioester hydrolysis and release coenzyme A. This ensures that the energy released from the thioester bond cleavage will drive the condensation.
^ abcGRCh38: Ensembl release 89: ENSG00000062485 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000005683 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ abWiegand G, Remington SJ (1986). "Citrate synthase: structure, control, and mechanism". Annual Review of Biophysics and Biophysical Chemistry. 15: 97–117. doi:10.1146/annurev.bb.15.060186.000525. PMID 3013232.
^ abGillen JB, Martin BJ, MacInnis MJ, Skelly LE, Tarnopolsky MA, Gibala MJ (2016). "Twelve Weeks of Sprint Interval Training Improves Indices of Cardiometabolic Health Similar to Traditional Endurance Training despite a Five-Fold Lower Exercise Volume and Time Commitment". PLOS One. 11 (4): e0154075. Bibcode:2016PLoSO..1154075G. doi:10.1371/journal.pone.0154075. PMC 4846072. PMID 27115137.
^MacInnis MJ, Zacharewicz E, Martin BJ, Haikalis ME, Skelly LE, Tarnopolsky MA, Murphy RM, Gibala MJ (2017). "Superior mitochondrial adaptations in human skeletal muscle after interval compared to continuous single-leg cycling matched for total work". The Journal of Physiology. 595 (9): 2955–2968. doi:10.1113/JP272570. PMC 5407978. PMID 27396440.
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