Abstract:
:Haloacid dehalogenases catalyse the removal of halides from organic haloacids and are of interest for bioremediation and for their potential use in the synthesis of industrial chemicals. We present the crystal structure of the homodimer DehI from Pseudomonas putida strain PP3, the first structure of a group I alpha-haloacid dehalogenase that can process both L- and D-substrates. The structure shows that the DehI monomer consists of two domains of approximately 130 amino acids that have approximately 16% sequence identity yet adopt virtually identical and unique folds that form a pseudo-dimer. Analysis of the active site reveals the likely binding mode of both L- and D-substrates with respect to key catalytic residues. Asp189 is predicted to activate a water molecule for nucleophilic attack of the substrate chiral centre resulting in an inversion of configuration of either l- or d-substrates in contrast to D-only enzymes. These details will assist with future bioengineering of dehalogenases.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Schmidberger JW,Wilce JA,Weightman AJ,Whisstock JC,Wilce MCdoi
10.1016/j.jmb.2008.02.035subject
Has Abstractpub_date
2008-04-18 00:00:00pages
284-94issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(08)00232-5journal_volume
378pub_type
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