Pyruvate dehydrogenase (acetyl-transferring)
|pyruvate dehydrogenase (acetyl-transferring)|
Pyruvate dehydrogenase E1 heterotetramer, Human
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
- pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
Thus, the two substrates of this enzyme are pyruvate and [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine, whereas its 3 products are dihydrolipoyllysine-residue acetyltransferase, S-acetyldihydrolipoyllysine, and CO2.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a disulfide as acceptor. The systematic name of this enzyme class is pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating). Other names in common use include MtPDC (mitochondrial pyruvate dehydogenase complex), pyruvate decarboxylase, pyruvate dehydrogenase, pyruvate dehydrogenase (lipoamide), pyruvate dehydrogenase complex, pyruvate:lipoamide 2-oxidoreductase (decarboxylating and, acceptor-acetylating), pyruvic acid dehydrogenase, and pyruvic dehydrogenase. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, alanine and aspartate metabolism, valine, leucine and isoleucine biosynthesis, pyruvate metabolism, and butanoate metabolism. It employs one cofactor, thiamin diphosphate.
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- Scriba P; Holzer H (1961). "Gewinnung von alphaHydroxyathyl-2-thiaminpyrophosphat mit Pyruvatoxydase aus Schweineherzmuskel". Biochem. Z. 334: 473–486.
- Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69 (1): 961–1004. PMID 10966480. doi:10.1146/annurev.biochem.69.1.961.
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