Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase - PubMed (original) (raw)
. 1993 Jun 24;363(6431):693-8.
doi: 10.1038/363693a0.
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- PMID: 8515812
- DOI: 10.1038/363693a0
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Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
K H Verschueren et al. Nature. 1993.
Free article
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.
Comment in
- Enzymes. Snapshots along the pathway.
Cygler M. Cygler M. Nature. 1993 Jun 24;363(6431):674-5. doi: 10.1038/363674a0. Nature. 1993. PMID: 8515808 No abstract available.
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