The enzyme catalyzes the conversion of GTP to dihydroneopterin triphosphate. It is a homodecamer and each subunit binds an essential zinc ion (PMID11087827).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 3316 A | ZN | zinc | zinc | mononuclear | Increases nucleophilicity Coordinates substrate Increases acidity |
*It refers to the MACiE reference pdb: 1fbx
| Metal/s Properties in Resting State | ||||||
| ZN 3316 A | Resting state enzyme (1fbx) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| References |
| -Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13567-72.(MEDLINE:11087827) |
| - Some information have been also deduced from the MACiE mechanism model |