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 α₂β₂ or (α₂β₂)₂ 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 Fe³⁺ 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.

中文翻译：

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2-Tyr-1-羧酸盐单核铁中心形成副球菌二甲基甲酰胺酶的活性位点。

N，N-二甲基甲酰胺（DMF）是一种广泛使用的有机溶剂，但也是一种有力的污染物。来自属的某些细菌物种，如副球菌，假单胞菌和产碱菌已进化为使用DMF作为唯一的碳和氮源，通过二甲基甲酰胺酶（DMFase）降解而生长。我们发现从DMFase副球菌属。应变DMF是包含多聚复合物的α的嗜盐和热稳定性酶₂ β ₂或（α ₂ β ₂）₂类型。大亚基和小亚基的三个结构域之一是迄今未描述的未知进化起源的蛋白质折叠。活性位点由单核铁和两个来自Glu的Tyr侧链酚盐和一个羧酸盐组成。活性位中的Fe ³⁺离子催化DMF中酰胺键的水解裂解。动力学表征表明该酶显示出亚基之间的协同作用，并且诱变和结构数据为催化机理提供了线索。