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-Structure paper
タイトル | A 2-Tyr-1-carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase. |
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ジャーナル・号・ページ | Angew Chem Int Ed Engl, Vol. 59, Issue 39, Page 16961-16966, Year 2020 |
掲載日 | 2020年9月21日 |
著者 | Chetan Kumar Arya / Swati Yadav / Jonathan Fine / Ana Casanal / Gaurav Chopra / Gurunath Ramanathan / Kutti R Vinothkumar / Ramaswamy Subramanian / |
PubMed 要旨 | N,N-dimethyl formamide (DMF) is an extensively used organic solvent but is also a potent pollutant. Certain bacterial species from genera such as Paracoccus, Pseudomonas, and Alcaligenes have evolved ...N,N-dimethyl formamide (DMF) is an extensively used organic solvent but is also a potent pollutant. Certain bacterial species from genera such as Paracoccus, Pseudomonas, and Alcaligenes have evolved to use DMF as a sole carbon and nitrogen source for growth via degradation by a dimethylformamidase (DMFase). We show that DMFase from Paracoccus sp. strain DMF is a halophilic and thermostable enzyme comprising a multimeric complex of the α β or (α β ) type. One of the three domains of the large subunit and the small subunit are hitherto undescribed protein folds of unknown evolutionary origin. The active site consists of a mononuclear iron coordinated by two Tyr side-chain phenolates and one carboxylate from Glu. The Fe ion in the active site catalyzes the hydrolytic cleavage of the amide bond in DMF. Kinetic characterization reveals that the enzyme shows cooperativity between subunits, and mutagenesis and structural data provide clues to the catalytic mechanism. |
リンク | Angew Chem Int Ed Engl / PubMed:32452120 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.8 - 3.2 Å |
構造データ | EMDB-0990, PDB-6lvd: EMDB-0991, PDB-6lve: PDB-6lvv: |
化合物 | ChemComp-FE: ChemComp-HOH: ChemComp-EDO: |
由来 |
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キーワード | HYDROLASE / ab polypeptide / mononuclear iron / amidohydrolase / tetramer / Amidase / Linear aliphatic amidohydrolase / metallo-amidase / heterotetramer. |