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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AFG8 | - |
- |
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 |