English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

4 Transand cis-1,3-dichloropropenes are active ingredients in widely used fumigants such as Telone II. These environmentally toxic dichloropropenes can be degraded by a number of soil bacteria such as Pseudomonas pavonaceae. The bacterial degradation of the 1,3-dichloropropene depends on a hydrolytic dehalogenation reaction catalyzed by both cisand trans-3-chloroacrylic acid dehalogenases. cis-3-Chloroacrylic acid dehalogenase is a member of the 4-OT family characterized by a conserved α-β-α motif and a catalytic N-terminal proline. Pro-1, Arg-70, Arg-73, and Glu-114 had initially been implicated as key catalytic residues in the cis-CaaD mechanism by amino acid sequence alignment with known members of the 4-OT family. Mutagenesis studies confirmed their importance prior to the availability of crystal structures. His-28 and Tyr-103 were identified as additional key catalytic residues based on recent crystal structures, and combined with the earlier results, led to a working hypothesis for the catalytic mechanism. Recent structures showed density for additional C-terminal residues and identified another active site residue, Arg-117. The importance of Arg-117 for activity has been confirmed by mutagenesis and kinetic studies on the R117A mutant. Furthermore, our structure shows a distinctly different conformation for the enzyme inactivated by (R)-Oxirane-2-carboxylate than that in the previously published structure, and adds to our understanding of the catalytic mechanism of cis-CaaD. This flexibility of the active site contributes to the diversity of substrates within the 4-OT family of enzymes. A summary of these results will be presented. This work is supported in part by grants from The Welch Foundation (F-1219 MLH; F-1334 CPW).

Crystal structure analysis of the oligo-peptide binding protein OppA complexed with peptides