The enzyme catalyzes the conversion of pyruvate to acetaldehyde in the penultimate step of alcohol fermentation. It performs the prototypical decarboxylation of 2-oxo acids using thiamin diphosphate (vitamin B1 coenzyme) and Mg(II) as cofactors PMID16853401.
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 558 A | MG | magnesium | magnesium | mononuclear | Coordinates cofactor |
*It refers to the MACiE reference pdb: 1pvd
| Metal/s Properties in Resting State | ||||||
| MG 558 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | The enzyme should not bind the cofactors in the resting state. | |||||
| References |
| -Wang J, Dong H, Li S, He H Theoretical study toward understanding the catalytic mechanism of pyruvate decarboxylase. J Phys Chem B. 2005 Oct 6;109(39):18664-72.(MEDLINE:16853401) |