Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsComposite Reactions
Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:
pyruvate dehydrogenaseInferred from experiment: aceE

Sub-reaction of:
1.2.1.-: pyruvate + coenzyme A + NAD+ → acetyl-CoA + CO2 + NADH

In Pathway: pyruvate decarboxylation to acetyl CoA

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: pyruvate dehydrogenase (acetyl-transferring)

Enzyme Commission Synonyms: 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

pyruvate + thiamine diphosphate + H+ = 2-(α-hydroxyethyl)thiamine diphosphate + CO2,
2-(α-hydroxyethyl)thiamine diphosphate + a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine = a [pyruvate dehydrogenase E2 protein] N6-S-acetyldihydrolipoyl-L-lysine + thiamine diphosphate

Enzyme Commission Summary:
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, dihydrolipoyllysine-residue acetyltransferase, which also binds multiple copies of EC, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC

This reaction is the sum of two individual reactions that are listed above.

Citations: [Perham00, SCRIBA61, OCHOA54]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reactions of [a [lipoyl-carrier protein] N6-dihydrolipoyl-L-lysine + NAD+ = a [lipoyl-carrier protein]-N6-lipoyl-L-lysine + NADH + H+] (
i1: a [glycine-cleavage complex H protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ a [glycine-cleavage complex H protein] N6-lipoyl-L-lysine + NADH + H+ (

i2: a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (

i3: a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


OCHOA54: OCHOA S (1954). "Enzymic mechanisms in the citric acid cycle." Adv Enzymol Relat Subj Biochem 15;183-270. PMID: 13158180

Perham00: Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions." Annu Rev Biochem 69;961-1004. PMID: 10966480

SCRIBA61: SCRIBA P, HOLZER H (1961). "[Production of alpha-hydroxyethyl-2-thiamine pyrophosphate with pyruvate oxidase from pig heart muscle]." Biochem Z 334;473-86. PMID: 13749426

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.5 on Mon Nov 30, 2015, BIOCYC13B.