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Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis

Haloacid dehalogenases catalyse the cleavage of carbon − halogen bonds in halogenated organic acids. These enzymes are of high interest due to their potential applications in bioremediation and in synthesis of various industrial products. The efficiency of dehalogenases in various applications can b...

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Main Authors: Adamu, Aliyu, Abdul Wahab, Roswanira, Aliyu, Firdausi, Aminu, Aminu Hamza, Hamza, Mariya Musa, Huyop, Fahrul
Format: Article
Published: Elsevier Ltd 2020
Subjects:
QC Physics
Online Access:http://eprints.utm.my/id/eprint/86972/
http://dx.doi.org/10.1016/j.procbio.2020.02.002
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spelling my.utm.869722020-10-22T04:21:45Z http://eprints.utm.my/id/eprint/86972/ Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis Adamu, Aliyu Abdul Wahab, Roswanira Aliyu, Firdausi Aminu, Aminu Hamza Hamza, Mariya Musa Huyop, Fahrul QC Physics Haloacid dehalogenases catalyse the cleavage of carbon − halogen bonds in halogenated organic acids. These enzymes are of high interest due to their potential applications in bioremediation and in synthesis of various industrial products. The efficiency of dehalogenases in various applications can be enhanced, provided that their molecular catalytic mechanisms are fully understood. Herein, we review the current understanding of enzymatic haloacid dehalogenation mechanisms and the important amino acid residues that are necessary for the enzyme’s catalysis, with special emphasis on haloacid dehalogenases produced by Rhizobium sp. Elsevier Ltd 2020 Article PeerReviewed Adamu, Aliyu and Abdul Wahab, Roswanira and Aliyu, Firdausi and Aminu, Aminu Hamza and Hamza, Mariya Musa and Huyop, Fahrul (2020) Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis. Process Biochemistry, 92 . pp. 437-446. ISSN 1359-5113 http://dx.doi.org/10.1016/j.procbio.2020.02.002
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 QC Physics
spellingShingle QC Physics
Adamu, Aliyu
Abdul Wahab, Roswanira
Aliyu, Firdausi
Aminu, Aminu Hamza
Hamza, Mariya Musa
Huyop, Fahrul
Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis
description Haloacid dehalogenases catalyse the cleavage of carbon − halogen bonds in halogenated organic acids. These enzymes are of high interest due to their potential applications in bioremediation and in synthesis of various industrial products. The efficiency of dehalogenases in various applications can be enhanced, provided that their molecular catalytic mechanisms are fully understood. Herein, we review the current understanding of enzymatic haloacid dehalogenation mechanisms and the important amino acid residues that are necessary for the enzyme’s catalysis, with special emphasis on haloacid dehalogenases produced by Rhizobium sp.
format Article
author Adamu, Aliyu
Abdul Wahab, Roswanira
Aliyu, Firdausi
Aminu, Aminu Hamza
Hamza, Mariya Musa
Huyop, Fahrul
author_facet Adamu, Aliyu
Abdul Wahab, Roswanira
Aliyu, Firdausi
Aminu, Aminu Hamza
Hamza, Mariya Musa
Huyop, Fahrul
author_sort Adamu, Aliyu
title Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis
title_short Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis
title_full Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis
title_fullStr Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis
title_full_unstemmed Haloacid dehalogenases of Rhizobium sp. and related enzymes: Catalytic properties and mechanistic analysis
title_sort haloacid dehalogenases of rhizobium sp. and related enzymes: catalytic properties and mechanistic analysis
publisher Elsevier Ltd
publishDate 2020
url http://eprints.utm.my/id/eprint/86972/
http://dx.doi.org/10.1016/j.procbio.2020.02.002
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score 13.160551

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