1MPY

STRUCTURE OF CATECHOL 2,3-DIOXYGENASE (METAPYROCATECHASE) FROM PSEUDOMONAS PUTIDA MT-2

1MPY の概要

• エントリーDOI: 10.2210/pdb1mpy/pdb
• 分子名称: CATECHOL 2,3-DIOXYGENASE, FE (II) ION, ACETONE, ... (4 entities in total)
• 機能のキーワード: catechol 2, 3-dioxygenase, extradiol dioxygenase, non heme iron dioxygenase, metapyrocatechase, oxidoreductase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 141270.87

構造登録者

Kita, A.,Kita, S.,Fujisawa, I.,Inaka, K.,Ishida, T.,Horiike, K.,Nozaki, M.,Miki, K. (登録日: 1998-10-20, 公開日: 1999-05-18, 最終更新日: 2024-02-14)

主引用文献

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

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: 10368270
DOI: 10.1016/S0969-2126(99)80006-9

実験手法

X-RAY DIFFRACTION (2.8 Å)