The enzyme catalyzes the thiamine PPi- and Mg2+-dependent decarboxylation of pyruvate to acetaldehyde and carbon dioxide (PMID10919763).
![Image of [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine](/thornton-srv/databases/MACiE/images/C15972.gif)
![Image of [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine](/thornton-srv/databases/MACiE/images/C16255.gif)
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 1368 C | MG | magnesium | magnesium | mononuclear | Coordinates cofactor |
*It refers to the MACiE reference pdb: 1w85
| Metal/s Properties in Resting State | ||||||
| MG 1368 C | Resting state enzyme (1w88) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21.(MEDLINE:12651851) |