1MPY
STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2
Summary for 1MPY
| Entry DOI | 10.2210/pdb1mpy/pdb |
| Descriptor | CATECHOL 2,3-DIOXYGENASE, FE (II) ION, ACETONE, ... (4 entities in total) |
| Functional Keywords | catechol 2, 3-dioxygenase, extradiol dioxygenase, non heme iron dioxygenase, metapyrocatechase, oxidoreductase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 4 |
| Total formula weight | 141270.87 |
| Authors | Kita, A.,Kita, S.,Fujisawa, I.,Inaka, K.,Ishida, T.,Horiike, K.,Nozaki, M.,Miki, K. (deposition date: 1998-10-20, release date: 1999-05-18, Last modification date: 2024-02-14) |
| Primary citation | 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 Fold.Des., 7:25-34, 1999 Cited by PubMed Abstract: Catechol dioxygenases catalyze the ring cleavage of catechol and its derivatives in either an intradiol or extradiol manner. These enzymes have a key role in the degradation of aromatic molecules in the environment by soil bacteria. Catechol 2, 3-dioxygenase catalyzes the incorporation of dioxygen into catechol and the extradiol ring cleavage to form 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase (metapyrocatechase, MPC) from Pseudomonas putida mt-2 was the first extradiol dioxygenase to be obtained in a pure form and has been studied extensively. The lack of an MPC structure has hampered the understanding of the general mechanism of extradiol dioxygenases. PubMed: 10368270DOI: 10.1016/S0969-2126(99)80006-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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