Literature summary for 1.2.1.104 extracted from

Park, Y.H.; Wei, W.; Zhou, L.; Nemeria, N.; Jordan, F.
Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit (2004), Biochemistry, 43, 14037-14046 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D15A	variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay	Escherichia coli
D7A	variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay	Escherichia coli
D9A	variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay	Escherichia coli
E12D	variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay	Escherichia coli
E12Q	variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay	Escherichia coli
I11A	variant is able to form a complex with the E2 component, and produce NADH in the overall assay	Escherichia coli
additional information	construction of deletion mutants of the E1 pyruvate dehydrogenase component lacking amino acids 6-15, 16-25, 26-35, 36-45, and 46-55, along with single-site substitutions at Asp7, Asp9, Pro10, Ile11, Glu12, Thr13, Arg14, and Asp15. The decarboxylation of pyruvate and the ability of PDHc-E1 to dimerize are not affected by any of the deletions or substitutions. Deletion mutant 46-55 and the Pro10Ala, Ile11Ala, and Thr13Ala variants are able to form a complex with the E2 component, and produce NADH in the overall assay, deletion mutants 16-25, 26-35, and 36-45 and the Asp7Ala, Asp9Ala, Glu12Gln, Glu12Asp, Arg14Ala, and Asp15Ala variants fail in both. All constructs can carry out reductive acetylation of the Escherichia coli lipoyl domain and reductively acetylate the Escherichia coli E2 component	Escherichia coli
P10A	variant is able to form a complex with the E2 component, and produce NADH in the overall assay	Escherichia coli
R14A	variant is neither able to form a complex with the E2 component, nor to produce NADH in the overall assay	Escherichia coli
T13A	variant is able to form a complex with the E2 component, and produce NADH in the overall assay	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AFG8 and P06959 and P0A9P0	P0AFG8 i.e. component E1/AceE, cf. EC 1.2.4.1, P06959 i.e. component E2/AceF, cf. EC 2.3.1.12, P0A9P0 i.e. component E3/LpdA, cf. EC 1.8.1.4	-

Synonyms

Synonyms	Comment	Organism
aceE	-	Escherichia coli
AceF	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	there are at least two loci of interaction between the E1 and E2 subunits: the thiamin diphosphate-bound substrate on E1 and the lipoylamide of E2, as reflected by the ability to reductively acetylate the latter and amino terminal residues 1-45 of E1 with regions of E2	Escherichia coli

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Release 2023.1 (January 2023)