The enzyme catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of dioxygen. It is an homo-tetramer and each subunit binds a ferrous ion (PMID10368270).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| FE2 308 A | FE | iron | iron | mononuclear | Coordinates substrate One electron donor Electrostatic stabiliser One electron acceptor |
*It refers to the MACiE reference pdb: 1mpy
| Metal/s Properties in Resting State | ||||||
| FE2 308 A | Resting state enzyme (1mpy) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | squarePyramidal | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| References |
| -Kita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2. Structure. 1999 Jan 15;7(1):25-34.(MEDLINE:10368270) |