Pyruvate dehydrogenase (acetyl-transferring)
|pyruvate dehydrogenase (acetyl-transferring)|
Pyruvate dehydrogenase E1 heterotetramer, Human
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
- 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 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, thiamine diphosphate.
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.
- Ochoa S (1954). "Enzymic mechanisms in the citric acid cycle". Advances in Enzymology and Related Subjects of Biochemistry. 15: 183–270. PMID 13158180.
- 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". Annual Review of Biochemistry. 69 (1): 961–1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.
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