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

Adamu, Aliyu; Wahab, Roswanira Abdul; Aliyu, Firdausi; Razak, Fazira Ilyana Abdul; Mienda, Bashir Sajo; Shamsir, Mohd Shahir; Huyop, Fahrul

doi:10.1016/j.jmgm.2019.07.012

Cited by 5 publications

(2 citation statements)

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“…The 2-haloacid dehalogenases show typical stereoselectivity; however, little is known about the stereoselective mechanism. The enantioselective mechanism of L-DEX has been studied using quantum mechanics/molecular mechanics (QM/MM) and fragment molecular orbital calculation (Kondo et al, 2015;Adamu et al, 2019), which have confirmed that the high activation energy barrier prevents this enzyme from acting on the D-substrate. However, it is still unclear how selectivity of enzymes on chiral substrates is regulated.…”

Section: Discussion and Prospectsmentioning

confidence: 90%

Mini Review: Advances in 2-Haloacid Dehalogenases

et al. 2021

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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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Section: Discussion and Prospectsmentioning

confidence: 90%

Mini Review: Advances in 2-Haloacid Dehalogenases

et al. 2021

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“…Studies of haloacid dehalogenases showed that they have conserved essential residues in its catalytic site and determined substrate binding [7,10] and enantioselectivity [4,16]. Furthermore, the size of active site on haloacid dehalogenase affects the range of its substrates [17].…”

Section: Introductionmentioning

confidence: 99%

In Silico Analysis on the Interaction of Haloacid Dehalogenase from Bacillus cereus IndB1 with 2-Chloroalkanoic Acid Substrates

Ratnaningsih

Saepulloh²

2022

The Scientific World Journal

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Recently, haloacid dehalogenases have gained a lot of interest because of their potential applications in bioremediation and synthesis of chemical products. The haloacid dehalogenase gene from Bacillus cereus IndB1 (bcfd1) has been isolated, expressed, and Bcfd1 enzyme activity towards monochloroacetic acid has been successfully studied. However, the structure, enantioselectivity, substrate range, and essential residues of Bcfd1 have not been elucidated. This research performed computational studies to predict the Bcfd1 protein structure and analyse the interaction of Bcfd1 towards several haloacid substrates to comprehend their enantioselectivity and substrates’ range. Structure prediction revealed that Bcfd1 protein consist of two domains. The main domain consists of seven β-sheets connected by six α-helices and four 310-helices forming a Rossmannoid fold. On the other hand, the cap domain consists of five β-sheets connected by five α-helices. The docking simulation showed that 2-chloroalkanoic acids bind to the active site of Bcfd1 with docking energy decreases as the length of their alkyl chain increases. The docking simulation also indicated that the docking energy differences of two enantiomers of 2-chloroalkanoic acids substrates were not significant. Further analysis revealed the role of Met1, Asp2, Cys33, and Lys204 residues in orienting the carboxylic group of 2-chloroalkanoic acids in the active site of this enzyme through hydrogen bonds. This research proved that computational studies could be used to figure out the effect of substrates enantiomer and length of carbon skeleton to Bcfd1 affinity toward 2-chloroalkanoic acids.

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