Publication details
Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels.
| Authors | |
|---|---|
| Year of publication | 2010 |
| Type | Article in Periodical |
| Magazine / Source | ACTA CRYSTALLOGRAPHICA D |
| MU Faculty or unit | |
| Citation | |
| Web | http://loschmidt.chemi.muni.cz/peg/pdf/acsf10a.pdf |
| Field | Biochemistry |
| Keywords | haloalkane dehalogenase DhaA ; Rhodococcus rhodochrous NCIMB 13064; hydrolytic degradation; 1.2.3-trichloropropane (TCP) |
| Description | The haloalkane dehalogenase DhaA from Rhodococcus rhodochrous NCIMB 13064 is a bacterial enzyme that shows catalytic activity for the hydrolytic degradation of the highly toxic industrial pollutant 1,2,3-trichloropropane (TCP). Mutagenesis focused on the access tunnels of DhaA produced protein variants with significantly improved activity towards TCP. Three mutants of DhaA named DhaA04 (C176Y), DhaA14 (I135F) and DhaA15 (C176Y + I135F) were constructed in order to study the functional relevance of the tunnels connecting the buried active site of the protein with the surrounding solvent. All three protein variants were crystallized using the sitting-drop vapour-diffusion technique. |
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