Structure and mechanism of bacterial dehalogenases: different ways to cleave a carbon-halogen bond.
The dehalogenases make use of fundamentally different strategies to cleave carbon-halogen bonds. The structurally characterized haloalkane dehalogenases, haloacid dehalogenases and 4-chlorobenzoate-coenzyme A dehalogenases use substitution mechanisms that proceed via a covalent aspartyl intermediate. Recent X-ray crystallographic analysis of a haloalcohol dehalogenase and a trans-3-chloroacrylic acid dehalogenase has provided detailed insight into a different intramolecular substitution mechanism and a hydratase-like mechanism, respectively. The available information on the various dehalogenases supports different views on the possible evolutionary origins of their activities.
de Jong
René M
RM
Department of Biophysical Chemistry, University of Groningen, Nijenborgh 4, NL-9747 AG Groningen, The Netherlands.
Dijkstra
Bauke W
BW
D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D002244:Carbon / Q000737:chemistry*; D004789:Enzyme Activation; D006219:Halogens / Q000737:chemistry*; D006867:Hydrolases / Q000737:chemistry*; D006868:Hydrolysis; D008958:Models, Molecular; D011485:Protein Binding; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D006219:Halogens; D002244:Carbon; D006867:Hydrolases; C084333:4-chlorobenzoyl coenzyme A dehalogenase; C034507:2-haloacid dehalogenase; C046137:haloalkane dehalogenase