Literature summary for 1.2.1.104 extracted from

Jones, D.D.; Stott, K.M.; Reche, P.A.; Perham, R.N.
Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex (2001), J. Mol. Biol., 305, 49-60 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P06959	P06959 i.e. dihydrolipoyllysine-residue acetyltransferase component, cf. EC. 2.3.1.12	-

General Information

General Information	Comment	Organism
physiological function	residues in the lipoyl-lysine beta-turn region of the unlipoylated subunit E2p lipoyl domain undergo significant changes in both chemical shift and transverse relaxation time in the presence of subunit E1p but not E1o. Residue Gly11, in a prominent surface loop between beta-strands 1 and 2 in the E2p lipoyl domain, also undergoes a significant change in chemical shift. Addition of pyruvate to the mixture of unlipoylated E2p lipoyl domain and E1p causes larger changes in chemical shift and the appearance of multiple cross-peaks for certain residues. Residues in both beta-strands 4 and 5, together with those in the prominent surface loop and the following beta-strand 2, interact with E1p. The values of transverse relaxation time across the polypeptide chain backbone are lower than in the presence of E1p alone. The lipoylated domain E2p exhibits significant changes in chemical shift and decreases in the overall transverse relaxation times in the presence of E1p, the residues principally affected being restricted to the half of the domain that contains the lipoyl-lysine (Lys41) residue	Escherichia coli

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Release 2023.1 (January 2023)