The enzyme catalyzes the convertion of a broad spectrum of aldose sugars into the corresponding lactones which are hydrolyzed to the aldonic acids. It is a dimer and each subunit binds three calcium ions: two involved in dimerization of the subunits, one involved in the catalytic reaction (PMID12686124).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| CA 1003 A | CA | calcium | calcium | mononuclear | Coordinates cofactor Increases electrophilicity Electrostatic stabiliser Increases acidity |
*It refers to the MACiE reference pdb: 1c9u
| Metal/s Properties in Resting State | ||||||
| CA 1003 A | Resting state enzyme (1qbi) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| References |
| -Oubrie A, Rozeboom HJ, Kalk KH, Olsthoorn AJ, Duine JA, Dijkstra BW Structure and mechanism of soluble quinoprotein glucose dehydrogenase. EMBO J. 1999 Oct 1;18(19):5187-94.(MEDLINE:10508152) |
| - Some information have been also deduced from the MACiE mechanism model |