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• W3102945423 abstract "Glutathione S-transferases (GSTs) are a family of enzymes that function in thedetoxification of a variety of electrophilic substrates. In this study, cloning andbiochemical characterization of GSTs from Acidovorax sp. KKS102 were carried out.Database suggests that there are eleven putative GSTs in Acidovorax sp. KKS102.Phylogenetic analysis showed that the GSTs were distributed into Beta, Nu, zeta, Chi,while some did not show any particular class. Two GSTs (KKSG6 and KKSG9) wereselected for further study. Sequence alignment showed that KKSG6 is closely related toBphK, a GST found within the operon responsible for PCB biodegradation in someorganisms and showed dechlorination function against metabolites of polychlorobiphenyldegradation. The substrate specificity of KKSG6 included reacting with CDNB,ethacrynic acid, hydrogen peroxide and cumene hydroperoxide. Molecular docking,sequence alignment, and site-directed mutagenesis studies revealed some key amino acidsthat were found to play a crucial role in the catalytic activity of the protein. The C10F andA180P mutants displayed an increase in catalytic activity of the enzyme against CDNBand ethacrynic, however, the peroxidase activities did not show any significant change.In contrast, the K107T mutant displayed variable results toward various substratessuggesting its possible role in determining substrate specificity in this enzyme. Analysisof kinetic parameters using CDNB and GSH as substrates showed a high Km value of theenzyme for CDNB when compared to GSH. C10F and A180P mutants also displayed adecrease in the affinity of both CDNB and GSH to KKSG6 with a corresponding increasein Vmax and kcat, however, K107T showed decrease in Vmax and kcat. The enzyme also displayed dechlorination function against 2, 3, and 4-chlorobenzoates and 2,4-dichlorobenzoate. The C10F and A180P mutants both showed an increase indechlorination function while K107T showed a variable result. The same trend ofdechlorination activity was observed against DDT, endosulfan, and permethrin.Phylogenetic analysis revealed that KKSG9 is closely related to zeta class, however, ithas possessed low sequence similarity to known zeta class GSTs. Functional analysisshowed that the enzyme exhibits wider substrate specificity compared to most zeta classGSTs by reacting with 1-chloro-2,4-dinitrobenzene (CDNB), p-nitrobenzyl chloride(NBC), ethacrynic acid (EA), hydrogen peroxide, and cumene hydroperoxide. Theenzyme also displayed dehalogenation function against dichloroacetate in addition topermethrin, and dieldrin. The mutant (Y12C) displayed low catalytic activity anddehalogenation function against all the substrates when compared with the wild type.Kinetic analysis using NBC and GSH as substrates showed that the mutant (Y12C)displayed a higher affinity for NBC when compared with the wild type, however, nosignificant change in GSH affinity was observed. The presence of a tyrosine residue inKKSG9 motif instead of commonly known Cys, Thr, Ser or Ala might represent anevolutionary trend toward improving the catalytic activity of the enzyme. These enzymescould be useful in the bioremediation of various classes of organochlorine pollutants." @default.
• W3102945423 created "2020-11-23" @default.
• W3102945423 creator A5066538495 @default.
• W3102945423 date "2018-06-01" @default.
• W3102945423 modified "2023-09-27" @default.
• W3102945423 title "Molecular cloning, expression and enzymatic characterization of cytosolic glutathione stransferase from Acidovorax sp. KKS102 / Dayyabu Shehu" @default.
• W3102945423 hasPublicationYear "2018" @default.
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