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Mini Review: Advances in 2-Haloacid Dehalogenases

The 2-haloacid dehalogenases (EC 3.8.1.X) are industrially important enzymes that catalyze the cleavage of carbon–halogen bonds in 2-haloalkanoic acids, releasing halogen ions and producing corresponding 2-hydroxyl acids. These enzymes are of particular interest in environmental remediation and envi...

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Autores principales: Wang, Yayue, Xiang, Qiao, Zhou, Qingfeng, Xu, Jingliang, Pei, Dongli
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8554231/
https://www.ncbi.nlm.nih.gov/pubmed/34721367
http://dx.doi.org/10.3389/fmicb.2021.758886
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author Wang, Yayue
Xiang, Qiao
Zhou, Qingfeng
Xu, Jingliang
Pei, Dongli
author_facet Wang, Yayue
Xiang, Qiao
Zhou, Qingfeng
Xu, Jingliang
Pei, Dongli
author_sort Wang, Yayue
collection PubMed
description The 2-haloacid dehalogenases (EC 3.8.1.X) are industrially important enzymes that catalyze the cleavage of carbon–halogen bonds in 2-haloalkanoic acids, releasing halogen ions and producing corresponding 2-hydroxyl acids. These enzymes are of particular interest in environmental remediation and environmentally friendly synthesis of optically pure chiral compounds due to their ability to degrade a wide range of halogenated compounds with astonishing efficiency for enantiomer resolution. The 2-haloacid dehalogenases have been extensively studied with regard to their biochemical characterization, protein crystal structures, and catalytic mechanisms. This paper comprehensively reviews the source of isolation, classification, protein structures, reaction mechanisms, biochemical properties, and application of 2-haloacid dehalogenases; current trends and avenues for further development have also been included.
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spelling pubmed-85542312021-10-30 Mini Review: Advances in 2-Haloacid Dehalogenases Wang, Yayue Xiang, Qiao Zhou, Qingfeng Xu, Jingliang Pei, Dongli Front Microbiol Microbiology The 2-haloacid dehalogenases (EC 3.8.1.X) are industrially important enzymes that catalyze the cleavage of carbon–halogen bonds in 2-haloalkanoic acids, releasing halogen ions and producing corresponding 2-hydroxyl acids. These enzymes are of particular interest in environmental remediation and environmentally friendly synthesis of optically pure chiral compounds due to their ability to degrade a wide range of halogenated compounds with astonishing efficiency for enantiomer resolution. The 2-haloacid dehalogenases have been extensively studied with regard to their biochemical characterization, protein crystal structures, and catalytic mechanisms. This paper comprehensively reviews the source of isolation, classification, protein structures, reaction mechanisms, biochemical properties, and application of 2-haloacid dehalogenases; current trends and avenues for further development have also been included. Frontiers Media S.A. 2021-10-15 /pmc/articles/PMC8554231/ /pubmed/34721367 http://dx.doi.org/10.3389/fmicb.2021.758886 Text en Copyright © 2021 Wang, Xiang, Zhou, Xu and Pei. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Wang, Yayue
Xiang, Qiao
Zhou, Qingfeng
Xu, Jingliang
Pei, Dongli
Mini Review: Advances in 2-Haloacid Dehalogenases
title Mini Review: Advances in 2-Haloacid Dehalogenases
title_full Mini Review: Advances in 2-Haloacid Dehalogenases
title_fullStr Mini Review: Advances in 2-Haloacid Dehalogenases
title_full_unstemmed Mini Review: Advances in 2-Haloacid Dehalogenases
title_short Mini Review: Advances in 2-Haloacid Dehalogenases
title_sort mini review: advances in 2-haloacid dehalogenases
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8554231/
https://www.ncbi.nlm.nih.gov/pubmed/34721367
http://dx.doi.org/10.3389/fmicb.2021.758886
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