Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number:

Enzymes and Genes:
AceF Inferred from experiment : aceF

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

In Pathway: pyruvate decarboxylation to acetyl CoA

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: dihydrolipoyllysine-residue acetyltransferase

Enzyme Commission Synonyms: acetyl-CoA:dihydrolipoamide S-acetyltransferase, dihydrolipoamide S-acetyltransferase, dihydrolipoate acetyltransferase, dihydrolipoic transacetylase, dihydrolipoyl acetyltransferase, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid acetyltransferase, lipoic transacetylase, lipoylacetyltransferase, thioltransacetylase A, transacetylase X, enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase, acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase

Enzyme Commission Summary:
A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC, pyruvate dehydrogenase (acetyl-transferring) and EC, dihydrolipoyl dehydrogenase. The lipoyl group of this enzyme is reductively acetylated by EC, and the only observed direction catalyzed by EC is that where the acetyl group is passed to coenzyme A.

Citations: [Brady54, Perham00, Gunsalus54, Gunsalus56]

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 [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [pyruvate dehydrogenase E2 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 [glycine-cleavage complex H protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ a [glycine-cleavage complex H protein] N6-lipoyl-L-lysine + NADH + H+ (

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


Brady54: Brady RO, Stadtman ER (1954). "Enzymatic thioltransacetylation." J Biol Chem 211(2);621-9. PMID: 13221570

Gunsalus54: Gunsalus IC (1954). "Group transfer and acyl-generating functions of lipoic acid derivatives." In: McElroy, W.D. and Glass, B. (Eds), A Symposium on the Mechanism of Enzyme Action, Johns Hopkins Press, Baltimore, pp. 545-580.

Gunsalus56: Gunsalus IC, Barton LS, Gruber W (1956). "Biosynthesis and structure of lipoic acid derivatives." J. Am. Chem. Soc. 78 1763-1766.

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

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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 19.0 on Tue Oct 13, 2015, biocyc13.