Arya, Chetan Kumar published the artcileA 2-Tyr-1-carboxylate Mononuclear Iron Center Forms the Active Site of a Paracoccus Dimethylformamidase, Application In Synthesis of 123-39-7, the main research area is dimethylformamidase iron center tyrosine Paracoccus; amide bond hydrolysis; bioremediation; dimethylforamamidase; metalloenzymes; protein structure.
N,N-DMF (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.
Angewandte Chemie, International Edition published new progress about Density functional theory. 123-39-7 belongs to class amides-buliding-blocks, name is N-Methylformamide, and the molecular formula is C2H5NO, Application In Synthesis of 123-39-7.
Referemce:
Amide – Wikipedia,
Amide – an overview | ScienceDirect Topics