Staff View: Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid

Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid

Dehalogenases continue to garner interest of the scientific community due to their potential applications in bioremediation of halogen-contaminated environment and in synthesis of various industrially relevant products. Example of such enzymes is DehL, an L-2-haloacid dehalogenase (EC 3.8.1.2) from...

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Main Authors:	Adamu, Aliyu, Abdul Wahab, Roswanira, Aliyu, Firdausi, Abdul Razak, Fazira Ilyana, Mienda, Bashir Sajo, Shamsir, Mohd. Shahir, Huyop, Fahrul
Format:	Article
Published:	Elsevier Inc. 2019
Subjects:	Q Science (General)
Online Access:	http://eprints.utm.my/id/eprint/89408/ http://dx.doi.org/10.1016/j.jmgm.2019.07.012
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spelling	my.utm.894082021-02-22T06:04:36Z http://eprints.utm.my/id/eprint/89408/ Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid Adamu, Aliyu Abdul Wahab, Roswanira Aliyu, Firdausi Abdul Razak, Fazira Ilyana Mienda, Bashir Sajo Shamsir, Mohd. Shahir Huyop, Fahrul Q Science (General) Dehalogenases continue to garner interest of the scientific community due to their potential applications in bioremediation of halogen-contaminated environment and in synthesis of various industrially relevant products. Example of such enzymes is DehL, an L-2-haloacid dehalogenase (EC 3.8.1.2) from Rhizobium sp. RC1 that catalyses the specific cleavage of halide ion from L-2-halocarboxylic acids to produce the corresponding D-2-hydroxycarboxylic acids. Recently, the catalytic residues of DehL have been identified and its catalytic mechanism has been fully elucidated. However, the enantiospecificity determinants of the enzyme remain unclear. This information alongside a well-defined catalytic mechanism are required for rational engineering of DehL for substrate enantiospecificity. Therefore, using quantum mechanics/molecular mechanics and molecular mechanics Poisson-Boltzmann surface area calculations, the current study theoretically investigated the molecular basis of DehL enantiospecificity. The study found that R51L mutation cancelled out the dehalogenation activity of DehL towards it natural substrate, L-2-chloropropionate. The M48R mutation, however introduced a new activity towards D-2-chloropropionate, conveying the possibility of inverting the enantiospecificity of DehL from L-to D-enantiomer with a minimum of two simultaneous mutations. The findings presented here will play important role in the rational design of DehL dehalogenase for improving substrate utility. Elsevier Inc. 2019-11 Article PeerReviewed Adamu, Aliyu and Abdul Wahab, Roswanira and Aliyu, Firdausi and Abdul Razak, Fazira Ilyana and Mienda, Bashir Sajo and Shamsir, Mohd. Shahir and Huyop, Fahrul (2019) Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid. Journal of Molecular Graphics and Modelling, 92 . pp. 131-139. ISSN 1093-3263 http://dx.doi.org/10.1016/j.jmgm.2019.07.012 DOI:10.1016/j.jmgm.2019.07.012
institution	Universiti Teknologi Malaysia
building	UTM Library
collection	Institutional Repository
continent	Asia
country	Malaysia
content_provider	Universiti Teknologi Malaysia
content_source	UTM Institutional Repository
url_provider	http://eprints.utm.my/
topic	Q Science (General)
spellingShingle	Q Science (General) Adamu, Aliyu Abdul Wahab, Roswanira Aliyu, Firdausi Abdul Razak, Fazira Ilyana Mienda, Bashir Sajo Shamsir, Mohd. Shahir Huyop, Fahrul Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid
description	Dehalogenases continue to garner interest of the scientific community due to their potential applications in bioremediation of halogen-contaminated environment and in synthesis of various industrially relevant products. Example of such enzymes is DehL, an L-2-haloacid dehalogenase (EC 3.8.1.2) from Rhizobium sp. RC1 that catalyses the specific cleavage of halide ion from L-2-halocarboxylic acids to produce the corresponding D-2-hydroxycarboxylic acids. Recently, the catalytic residues of DehL have been identified and its catalytic mechanism has been fully elucidated. However, the enantiospecificity determinants of the enzyme remain unclear. This information alongside a well-defined catalytic mechanism are required for rational engineering of DehL for substrate enantiospecificity. Therefore, using quantum mechanics/molecular mechanics and molecular mechanics Poisson-Boltzmann surface area calculations, the current study theoretically investigated the molecular basis of DehL enantiospecificity. The study found that R51L mutation cancelled out the dehalogenation activity of DehL towards it natural substrate, L-2-chloropropionate. The M48R mutation, however introduced a new activity towards D-2-chloropropionate, conveying the possibility of inverting the enantiospecificity of DehL from L-to D-enantiomer with a minimum of two simultaneous mutations. The findings presented here will play important role in the rational design of DehL dehalogenase for improving substrate utility.
format	Article
author	Adamu, Aliyu Abdul Wahab, Roswanira Aliyu, Firdausi Abdul Razak, Fazira Ilyana Mienda, Bashir Sajo Shamsir, Mohd. Shahir Huyop, Fahrul
author_facet	Adamu, Aliyu Abdul Wahab, Roswanira Aliyu, Firdausi Abdul Razak, Fazira Ilyana Mienda, Bashir Sajo Shamsir, Mohd. Shahir Huyop, Fahrul
author_sort	Adamu, Aliyu
title	Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid
title_short	Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid
title_full	Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid
title_fullStr	Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid
title_full_unstemmed	Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid
title_sort	theoretical analyses on enantiospecificity of l-2-haloacid dehalogenase (dehl) from rhizobium sp. rc1 towards 2-chloropropionic acid
publisher	Elsevier Inc.
publishDate	2019
url	http://eprints.utm.my/id/eprint/89408/ http://dx.doi.org/10.1016/j.jmgm.2019.07.012
_version_	1692991779359424512
score	13.211869

Theoretical analyses on enantiospecificity of L-2-haloacid dehalogenase (DehL) from Rhizobium sp. RC1 towards 2-chloropropionic acid

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