The enzyme catalyzes the convertion of 3-deoxy-D-arabino-heptulosonate 7-phosphate to dehydro-quinate (PMID9685163). It is a homodimer and each subunit binds a Zn2+ ion (PMID3157372).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 402 A | ZN | zinc | zinc | mononuclear | Coordinates substrate Increases acidity |
*It refers to the MACiE reference pdb: 1dqs
| Metal/s Properties in Resting State | ||||||
| ZN 402 A | Resting state enzyme (1xah) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | trigonalPyramidal | |||||
| Coordination Number | 3 | |||||
| Notes | - | |||||
| References |
| -Carpenter EP, Hawkins AR, Frost JW, Brown KA Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature. 1998 Jul 16;394(6690):299-302.(MEDLINE:9685163) |
| - Some information have been also deduced from the MACiE mechanism model |