The enzyme catalyzes the stereospecific hydroxylation of the glycine alpha-carbon of all the peptidylglycine substrates. It binds two copper ions largely separated in space (PMID10580705).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| CU 357 x | CU | copper | copper | mononuclear | One electron acceptor One electron donor |
| CU 358 x | CU | copper | copper | mononuclear | Coordinates substrate Electron relay |
*It refers to the MACiE reference pdb: 1sdw
| Metal/s Properties in Resting State | ||||||
| CU 357 x | Resting state enzyme (1phm) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tShaped | |||||
| Coordination Number | 3 | |||||
| Notes | - | |||||
| CU 358 x | Resting state enzyme (1phm) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| References |
| -Prigge ST, Eipper BA, Mains RE, Amzel LM, Science. 2004 May 7;304(5672):836-7. Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex. Science. 2004 May 7;304(5672):864-7.(MEDLINE:15131304) |
| -Chen P, Solomon EI Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site. J Am Chem Soc. 2004 Apr 21;126(15):4991-5000.(MEDLINE:15080705) |
| - Some information have been also deduced from the MACiE mechanism model |