Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 59, Issue 39, Pages 16961-16966Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202005332
Keywords
amide bond hydrolysis; bioremediation; dimethylforamamidase; metalloenzymes; protein structure
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Funding
- Council of Industrial and Scientific Research, India
- IIT Kanpur
- DBT [DBT/PR12422/MED/31/287/2014]
- Institute for Stem Cell Science and Regenerative Medicine (inStem)
- National Center for Biological Sciences (TIFR)
- Department of Biotechnology [BT/PR5081/INF/22/156/2012, BT/INF/22/SP22660/2017]
- SERB, India
- Department of Chemistry
- National Institutes of Health, National Center for Advancing Translational Sciences ASPIRE Design Challenge awards
- Indiana Clinical and Translational Sciences Institute from the National Institutes of Health, National Center for Advancing Translational Sciences [UL1TR002529]
- Purdue University Center for Cancer Research - National Institutes of Health [P30 CA023168]
- MRC
- Integrative Data Science Institute award at Purdue University
- MRC [MC_U105192715] Funding Source: UKRI
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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 fromParacoccussp. strain DMF is a halophilic and thermostable enzyme comprising a multimeric complex of the alpha(2)beta(2)or (alpha(2)beta(2))(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 Fe(3+)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.
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