Linked Life Data

18353360

Source:http://linkedlifedata.com/resource/pubmed/id/18353360

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-4-3
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
378
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
284-94
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The crystal structure of DehI reveals a new alpha-haloacid dehalogenase fold and active-site mechanism.
pubmed:affiliation
Department of Pharmacology, School of Medicine and Pharmacology, The University of Western Australia, Perth, Western Australia 6907, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't