2016
DOI: 10.1016/j.jbiosc.2015.09.008
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Environment-induced conformational and functional changes of l-2-haloacid dehalogenase

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Cited by 4 publications
(4 citation statements)
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“…Hpk6, hpk7, and hpk11 proteins, belonging to histidine protein kinase (HPK), have a regulatory function in the synthesis of plantaricins and are therefore crucial to the strains [61]. The deh gene encodes an L-2-haloacid dehalogenase, an enzyme that degrades halogenated compounds present in drugs and environmental pollutants such as chlorobenzene, chlorocyclohexane, chloroalkane, and chloroalkene [62]. This enzyme presents applications in chemical industries, bioremediation, and sustainable chemistry [60, 61].…”
Section: Resultsmentioning
confidence: 99%
“…Hpk6, hpk7, and hpk11 proteins, belonging to histidine protein kinase (HPK), have a regulatory function in the synthesis of plantaricins and are therefore crucial to the strains [61]. The deh gene encodes an L-2-haloacid dehalogenase, an enzyme that degrades halogenated compounds present in drugs and environmental pollutants such as chlorobenzene, chlorocyclohexane, chloroalkane, and chloroalkene [62]. This enzyme presents applications in chemical industries, bioremediation, and sustainable chemistry [60, 61].…”
Section: Resultsmentioning
confidence: 99%
“…L-DEX specifically acts on L-2-haloalkanoic acids to produce D-2-hydroxyalkanoic acids. These enzymes are widespread in nature and their biochemical characteristics and structures have been studied extensively (Satpathy et al, 2016;Wang et al, 2016;Adamu et al, 2020). So far, the three-dimensional (3D) structures of specific L-DEXs and their substrate complexes have been analyzed, including L-DEX YL from Pseudomonas sp.…”
Section: Structural Characteristics and Catalytic Mechanismmentioning
confidence: 99%
“…The aggregation of proteins often changes their secondary structure, for example in amyloid formation [ 15 , 16 ]. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectrometry are effective tools for the analysis of protein secondary structures to examine the mechanisms of protein aggregation and the change of protein activity [ [17] , [18] , [19] , [20] , [21] , [22] ]. For example, the secondary structure of amyloid-β 1-42 changes from a soluble monomer with a random coil form to an insoluble aggregate with a β-sheet structure, which can be monitored by the CD spectra [ 23 ].…”
Section: Introductionmentioning
confidence: 99%