Title : Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase - Verschueren_1993_Nature_363_693 |
Author(s) : Verschueren KH , Seljee F , Rozeboom HJ , Kalk KH , Dijkstra BW |
Ref : Nature , 363 :693 , 1993 |
Abstract :
Crystal structures of haloalkane dehalogenase were determined in the presence of the substrate 1,2-dichloroethane. At pH 5 and 4 degrees C, substrate is bound in the active site without being converted; warming to room temperature causes the substrate's carbon-chlorine bond to be broken, producing a chloride ion with concomitant alkylation of the active-site residue Asp124. At pH 6 and room temperature the alkylated enzyme is hydrolysed by a water molecule activated by the His289-Asp260 pair in the active site. These results show that catalysis by the dehalogenase proceeds by a two-step mechanism involving an ester intermediate covalently bound at Asp124. |
PubMedSearch : Verschueren_1993_Nature_363_693 |
PubMedID: 8515812 |
Gene_locus related to this paper: xanau-halo1 |
Substrate | 1,2-dichloroethane |
Gene_locus | xanau-halo1 |
Family | Haloalkane_dehalogenase-HLD1 |
Structure | 2DHC 2DHD 2DHE |
Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW (1993)
Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
Nature
363 :693
Verschueren KH, Seljee F, Rozeboom HJ, Kalk KH, Dijkstra BW (1993)
Nature
363 :693