The structural and functional studies of the non-stereospecific α-haloacid dehalogenase (DehE) from rhizobium sp. RC1
Environmental pollution caused by the abundance of xenobi otic compounds in nature. For instance, synthetically halogenated compounds released from chemical industry we re proven harmful to our health and environment. However, α-haloacid dehalogenases could catalysed the removal of halides from...
| Main Authors: | , , , , , |
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| Format: | Conference or Workshop Item |
| Language: | English English English |
| Published: |
2013
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| Subjects: | |
| Online Access: | http://irep.iium.edu.my/37058/ http://irep.iium.edu.my/37058/ http://irep.iium.edu.my/37058/1/79.pdf http://irep.iium.edu.my/37058/4/biomicroworld2013_participants_list.pdf http://irep.iium.edu.my/37058/7/BioMicroWorld2013-Book-of-Abstracts.pdf |
| Summary: | Environmental pollution caused by the abundance of xenobi
otic compounds in nature. For instance, synthetically
halogenated compounds released from chemical industry we
re proven harmful to our health and environment.
However, α-haloacid dehalogenases could catalysed the removal of halides from organic haloalkanoic acids and
of interest for bioremediation. This study presents the first structural conformations and important residues of the non-stereospecific α-haloacid dehalogenase, DehE from
Rhizobium sp. RC1. The enzyme was modeled using ‘in silico’technique and crystal structure of DehI from
Pseudomonas putida PP3 was used as a template since both
of them gets high similiarity to each other. DehE consis
ts of only helices motif and depicted active site showed
that the binding orientiations of both D- and L-2-chlor
opropionic acid by using substrate-docking analysis shared similar key binding residues among non-stereo specific α -haloacid dehalogenases. Twelve residues lining the active site has identified and some of them were verified using site-directed mutagenesis tests. Each residues was affected after mutation and Asp189 was proven to be as a catalytic residue for nucleophilic attack mechansim when its mutation resulted in total loss of activity.
Three binding residues, Trp34, Phe37 and Ser188 were
responsible for substrate recognition due to their mutati
on had diminish activity of the enzyme to below 20%.
These details will promote more protein engineering studies to α haloacid dehalogenases for future
bioremediation and industrial applications. |
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