Unknown

Dataset Information

0

Mini Review: Advances in 2-Haloacid Dehalogenases.


ABSTRACT: 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.

SUBMITTER: Wang Y 

PROVIDER: S-EPMC8554231 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature

altmetric image

Publications

Mini Review: Advances in 2-Haloacid Dehalogenases.

Wang Yayue Y   Xiang Qiao Q   Zhou Qingfeng Q   Xu Jingliang J   Pei Dongli D  

Frontiers in microbiology 20211015


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-hal  ...[more]

Similar Datasets

| S-EPMC10281000 | biostudies-literature
| S-EPMC179244 | biostudies-other
| S-EPMC8706862 | biostudies-literature
| S-EPMC4989007 | biostudies-literature
| S-EPMC9021918 | biostudies-literature
| S-EPMC8446533 | biostudies-literature
| S-EPMC1483214 | biostudies-literature
| S-EPMC8718671 | biostudies-literature
| S-EPMC4821368 | biostudies-literature
| S-EPMC6804260 | biostudies-literature