The enzyme catalyzes the conversion of tyrosine to dihydroxyphenylalanine. It is a homotetramer and each subunits binds a catalytic iron (PMID9228951).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| FE 501 x | FE | iron | iron | mononuclear | Coordinates substrate One electron donor One electron acceptor Electron pair donor Electron pair acceptor |
*It refers to the MACiE reference pdb: 2toh
| Metal/s Properties in Resting State | ||||||
| FE 501 x | Resting state enzyme (1toh) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | octahedral | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| References |
| -Fitzpatrick PF Mechanism of aromatic amino acid hydroxylation. Biochemistry. 2003 Dec 9;42(48):14083-91.(MEDLINE:14640675) |
| - Some information have been also deduced from the MACiE mechanism model |