EC Number   |
Reaction |
Reference |
|---|
    1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
- |
- |
| 1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
active center communication between the cofactors in the enzyme complex. Only one of the thiamine molecules bound to the two active sites is in a chemically activated state whereas the thiamin in the inactive states ionizes with a rate that is at least three orders of magnitude smaller. Model of an active site synchronization via a proton wire that keeps the two active sites in an alternating activation state |
672086 |
| 1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
active site interactions, reaction mechanism |
654647 |
| 1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
catalytic site is formed by the conserved residues Tyr281 and Arg282 |
655474 |
| 1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
reaction mechanism, role of water molecules |
654741 |
| 1.2.4.1 | 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 |
674563 |
| 1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
substrate channelling in the multienzyme complex rests on the recognition of the lipoyl domain by enzyme. Cofactor thiamine diphosphate and substrate pyruvate have distinct effects on enzyme/lipoyl domain interaction. conformational freedom is allowed by the linker in the movement of the lipoyl domain between active sites |
675426 |
| 1.2.4.1 | pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 |
two-step reaction: thiamine diphosphate dependent decarboxylation of pyruvate to 2-hydroxyethylidene-thiamine diphosphate and subsequent reductive acetylation of lipoic acid residues bound to the dihydrolipoamide acetyltransferase, EC 2.3.1.12 |
348983 |
