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Literature summary for 1.2.4.1 extracted from

  • Arjunan, P.; Sax, M.; Brunskill, A.; Chandrasekhar, K.; Nemeria, N.; Zhang, S.; Jordan, F.; Furey, W.
    A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct (2006), J. Biol. Chem., 281, 15296-15303.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with phosphonolactylthiamine diphosphate as structural and electrostatic analogue of alpha-lactylthiamin diphosphate. Presence of phosphonolactylthiamin diphosphate causes large conformational changes Escherichia coli

Protein Variants

Protein Variants Comment Organism
H407A crystallization data. Interaction between H407 and phosphonolactylthiamine diphosphate is essential for stabilization of two loop regions in the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFG8
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Reaction

Reaction Comment Organism Reaction ID
pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 reaction with phosphonolactylthiamine diphosphate gives a covalently bound, pre-decarboxylation reaction intermediate analogue tightly held in the active site through hydrogen bonds with H407, Y599, and H640 Escherichia coli