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Citrate synthase, mitochondrial (CS) from porcine (pig) heart is a dimeric enzyme comprising two identical subunits of 437 amino acids each, localized in mitochondria. It catalyzes the initial, rate-limiting step of the citric acid cycle by facilitating the condensation of oxaloacetate and acetyl-CoA to produce citrate. This reaction is essential for aerobic energy production in eukaryotes[1][5][2]. Porcine heart citrate synthase is a well-studied enzyme used as a model for structural and mechanistic analysis. It is subject to product inhibition and regulated by mitochondrial metabolites, and its inhibition can affect cellular energy status. The protein undergoes post-translational modification, such as trimethylation of lysine[3]. Fluctuations in its activity can reflect or contribute to metabolic disorders, particularly those affecting energy metabolism in cardiac tissues[1][5][3][2].
Competitive inhibition (e.g., by fluoroacetyl-CoA) Allosteric inhibition (e.g., by palmitoyl-CoA)
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