Conformational changes allow processing of bulky substrates by a haloalkane dehalogenase with a small and buried active site
نویسندگان
چکیده
منابع مشابه
Thermodynamic analysis of halide binding to haloalkane dehalogenase suggests the occurrence of large conformational changes.
Haloalkane dehalogenase (DhlA) hydrolyzes short-chain haloalkanes to produce the corresponding alcohols and halide ions. Release of the halide ion from the active-site cavity can proceed via a two-step and a three-step route, which both contain slow enzyme isomerization steps. Thermodynamic analysis of bromide binding and release showed that the slow unimolecular isomerization steps in the thre...
متن کاملKinetic analysis and X-ray structure of haloalkane dehalogenase with a modified halide-binding site.
Haloalkane dehalogenase (DhlA) catalyzes the hydrolysis of haloalkanes via an alkyl-enzyme intermediate. Trp175 forms a halogen/halide-binding site in the active-site cavity together with Trp125. To get more insight in the role of Trp175 in DhlA, we mutated residue 175 and explored the kinetics and X-ray structure of the Trp175Tyr enzyme. The mutagenesis study indicated that an aromatic residue...
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15 صفحه اولComputational site-directed mutagenesis of haloalkane dehalogenase in position 172.
The application of molecular modelling and quantum-chemistry calculations for the 'computational site-directed mutagenesis' of haloalkane dehalogenase is described here. The exhaustive set of single point mutants of haloalkane dehalogenase in position 172 was constructed by homology modelling. The ability of substituting residues to stabilize the halide ion formed during the dehalogenation reac...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2018
ISSN: 0021-9258
DOI: 10.1074/jbc.ra117.000328