The Enzyme Database

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EC 1.2.4.1     
Accepted name: pyruvate dehydrogenase (acetyl-transferring)
Reaction: pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
For diagram of oxo-acid-dehydrogenase complexes, click here
Glossary: dihydrolipoyl group
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): 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; pyruvic dehydrogenase
Systematic name: pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating)
Comments: Contains thiamine diphosphate. It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9014-20-4
References:
1.  Ochoa, S. Enzymic mechanisms in the citric acid cycle. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183–270. [PMID: 13158180]
2.  Scriba, P. and Holzer, H. Gewinnung von αHydroxyäthyl-2-thiaminpyrophosphat mit Pyruvatoxydase aus Schweineherzmuskel. Biochem. Z. 334 (1961) 473–486. [PMID: 13749426]
3.  Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [PMID: 10966480]
[EC 1.2.4.1 created 1961, modified 2003]
 
 


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