Title : Evolving haloalkane dehalogenases - Janssen_2004_Curr.Opin.Chem.Biol_8_150
Author(s) : Janssen DB
Ref : Curr Opin Chemical Biology , 8 :150 , 2004
Abstract :

Mechanistic insight into the biochemistry of carbon-halogen bond cleavage is rapidly growing because of recent structural, biochemical and computational studies that have provided further insight into how haloalkane dehalogenases achieve their impressive catalytic activity. An occluded water-free active-site cavity together with strong hydrogen bond donating groups reduce the transition state energy barrier compared with that of the non-enzymatic reaction in water. Even though all known haloalkane dehalogenases belong to the alpha/beta-hydrolase fold family, there are interesting differences in mechanistic and kinetic details, as shown by properties of mutant enzymes and transient-state kinetic studies. To improve enzymatic degradation of some environmentally important recalcitrant compounds, site-directed mutagenesis and directed-evolution studies are being done.

PubMedSearch : Janssen_2004_Curr.Opin.Chem.Biol_8_150
PubMedID: 15062775

Citations formats

Janssen DB (2004)
Evolving haloalkane dehalogenases
Curr Opin Chemical Biology 8 :150

Janssen DB (2004)
Curr Opin Chemical Biology 8 :150