The enzyme catalyzes the nonoxidative conversion of benzoylformate to benzaldehyde and carbon dioxide. It requires thiamin-diphosphate and a divalent metal ion to perform catalysis PMID9665697.
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| MG 529 A | MG | magnesium | divalent cation | mononuclear | Coordinates cofactor |
*It refers to the MACiE reference pdb: 1mcz
| Metal/s Properties in Resting State | ||||||
| MG 529 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Polovnikova ES, McLeish MJ, Sergienko EA, Burgner JT, Anderson NL, Bera AK, Jordan F, Kenyon GL, Hasson MS Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase. Biochemistry. 2003 Feb 25;42(7):1820-30.(MEDLINE:12590569) |