EC 184.108.40.206 - Pyruvate dehydrogenase (acetyl-transferring)
IntEnz Enzyme Nomenclature
pyruvate dehydrogenase (lipoamide)
pyruvate dehydrogenase complex
pyruvate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-acetylating)
pyruvic acid dehydrogenase
19189 [IUBMB][dihydrolipoyllysine-residue acetyltransferase]-(R)-N6-lipoyl-L-lysine[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-lipoyl-L-lysineGENERIC:10480Is ROOT: no
ROOT compound: GENERIC:10479Number of residues: 1H+H(+)Name origin: UniProt - CHECKED (C)Formula: H
Charge: 1ChEBI compound status: CHECKED (C)pyruvatepyruvateName origin: UniProt - CHECKED (C)Formula: C3H3O3
Charge: -1ChEBI compound status: CHECKED (C)<?>[dihydrolipoyllysine-residue acetyltransferase]-(R)-N6-(S8-acetyldihydrolipoyl)-L-lysine[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysineGENERIC:10481Is ROOT: no
ROOT compound: GENERIC:10479Number of residues: 1
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 220.127.116.11, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC 18.104.22.168, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 22.214.171.124.
Links to other databases
Enzymic mechanisms in the citric acid cycle.Adv. Enzymol. Relat. Subj. Biochem. 15: 183-270 (1954).
Gewinnung von α-Hydroxyäthyl-2-thiaminpyrophosphat mit Pyruvatoxydase aus Schweineherzmuskel.Biochem. Z. 334: 473-486 (1961).
Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.Annu. Rev. Biochem. 69: 961-1004 (2000). [PMID: 10966480]
[EC 126.96.36.199 created 1961, modified 2003]