Dehalogenation of an anthropogenic compound by an engineered variant of the mouse cytokine macrophage migration inhibitory factor

Anna A Wasiel; Bert-Jan Baas; Ellen Zandvoort; Wim J Quax; Gerrit J Poelarends

doi:10.1002/cbic.201200153

Dehalogenation of an anthropogenic compound by an engineered variant of the mouse cytokine macrophage migration inhibitory factor

Chembiochem. 2012 Jun 18;13(9):1270-3. doi: 10.1002/cbic.201200153. Epub 2012 May 21.

Authors

Anna A Wasiel¹, Bert-Jan Baas, Ellen Zandvoort, Wim J Quax, Gerrit J Poelarends

Affiliation

¹ Department of Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.

PMID: 22615048
DOI: 10.1002/cbic.201200153

Abstract

An unconventional dehalogenase: An engineered variant (I64V/V106L) of the mouse cytokine macrophage migration inhibitory factor (MIF) promiscuously catalyzes the hydrolytic dehalogenation of the xenobiotic organohalogen trans-3-chloroacrylic acid to acetaldehyde. Although the dehalogenase activity of this MIF variant is quite low, it achieves an ~10(9) -fold rate enhancement, matching those of conventional enzymes acting on their natural substrates.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acrylates / chemistry
Acrylates / metabolism*
Animals
Halogenation*
Kinetics
Macrophage Migration-Inhibitory Factors / chemistry
Macrophage Migration-Inhibitory Factors / genetics*
Macrophage Migration-Inhibitory Factors / metabolism*
Mice
Models, Molecular
Mutant Proteins / chemistry
Mutant Proteins / genetics*
Mutant Proteins / metabolism*
Protein Conformation
Protein Engineering*

Substances

Acrylates
Macrophage Migration-Inhibitory Factors
Mutant Proteins
3-chloroacrylic acid