Functional classification and biochemical characterization of a novel rho class glutathione<i>S</i>‐transferase in<i>Synechocystis</i> PCC 6803

Pandey, Tripti; Chhetri, Gaurav; Chinta, Ramesh; Kumar, Bijay; Singh, Dev Bukhsh; Tripathi, Timir; Singh, Arvind

doi:10.1016/j.fob.2014.11.006

Cited by 18 publications

(18 citation statements)

References 32 publications

(35 reference statements)

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“…In bacteria, in addition to the previously known cytosolic beta, Chi, Zeta, and Theta classes, three additional classes of Rho, Eta, and Nu were recently discovered [7][8][9]17]. One major criterion for classifying cytosolic GSTs is the use of percentage sequence similarity, which is generally agreed that proteins which shared 40% and above, the sequence similarity belongs to the same class, while those with less than 20% are classified into a different class [21].…”

Section: Structure and Phylogenetic Relationship Of Cytosolic Glutathmentioning

confidence: 99%

“…Furthermore, while the average molecular weight of cytosolic GSTs is around 25KDa, this protein was found to have a molecular weight of about 30KDa. Biochemical characterization showed that the enzyme has strong dehalogenase activity toward dichloro-acetate and glutathione-dependent peroxidase activity [7].…”

Section: Rho Class Gstsmentioning

confidence: 99%

“…Despite the fact that zeta class GSTs are widely distributed in mammals, plants, fungi, and bacteria, the reports of dichloroacetate dechlorinating activity of this class of GST was only investigated thoroughly in mammalian species. In bacteria, a newly discovered Rho class GST from Synechocystis PCC 6803 was found to have a dichloroacetate dechlorinating activity against DCA in a similar manner to zeta class GST [7]. The proposed mechanism of the reaction involves glutathione-catalyzed dehalogenation of DCA to form glyoxylate.…”

Section: Dehalogenation Of Dichloroacetatementioning

confidence: 99%

“…Advances in gene sequencing techniques also continued to provide insight into new classes of cGSTs in bacteria with novel functions. Currently, seven different classes were already identified in bacteria, with some of them playing a valuable role in the biodegradation of several classes of pollutants [5,[7][8][9].…”

Section: Introductionmentioning

confidence: 99%

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Cytosolic Glutathione S-transferase in Bacteria: A Review

Shehu¹,

Abdullahi²,

Alias³

2018

Pol. J. Environ. Stud.

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Cytosolic glutathione S-transferase in bacteria possesses the biochemical capacity to degrade various classes of organochlorine pollutants in the environment in addition to their primary role of defending the organism from a wide range of endobiotics and xenobiotic substrates. Furthermore, the ability of different classes of cGST to recognize a wide repertoire of substrates due the variability in the substrate binding site of the enzymes makes them well suited for bioremediation purposes. cGSTs act as dehalogenases promoting a rapid degradation of various organochlorine compounds. Dehalogenation served as the primary mechanism for detoxification of various organochlorine compounds, making them vulnerable to attack by other degradative enzymes. However, despite their potential and advantage of wide substrate specificity, cGSTs have not been exploited for bioremediation purposes. In this review, we described the various cGST classes in bacteria and their phylogenetic relationships. Furthermore, the review reiterated that cGSTs in bacteria are involved in dehalogenation reaction, and this property can be harnessed for bioremediation of a diverse class of organochlorine pollutants as they currently represent the largest class of pollutants in the environment.

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Section: Structure and Phylogenetic Relationship Of Cytosolic Glutathmentioning

confidence: 99%

Section: Rho Class Gstsmentioning

confidence: 99%

Section: Dehalogenation Of Dichloroacetatementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Cytosolic Glutathione S-transferase in Bacteria: A Review

Shehu¹,

Abdullahi²,

Alias³

2018

Pol. J. Environ. Stud.

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“…GSTs are classified into four major groups based on substrate specificity: cytosolic GSTs, kappa-class GSTs (mitochondrial), membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG, microsomal), and bacterial fosfomycin-resistant proteins 14 – 17 . The cytosolic GSTs are more abundant and can be further divided into several classes like mu, alpha, pi, theta, sigma, zeta, omega, nu, lambda, phi, tau, delta, epsilon, iota, chi, and rho 10 , 12 , 18 – 25 . Structurally, most of the GSTs are dimeric that can be either homodimer or heterodimer.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive analysis of the catalytic and structural properties of a mu-class glutathione s-transferase from Fasciola gigantica

Kalita

Shukla

et al. 2017

Sci Rep

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Glutathione S‒transferases (GSTs) play an important role in the detoxification of xenobiotics. They catalyze the nucleophilic addition of glutathione (GSH) to nonpolar compounds, rendering the products water-soluble. In the present study, we investigated the catalytic and structural properties of a mu-class GST from Fasciola gigantica (FgGST1). The purified recombinant FgGST1 formed a homodimer composed of 25 kDa subunit. Kinetic analysis revealed that FgGST1 displays broad substrate specificity and shows high GSH conjugation activity toward 1-chloro-2,4-dinitrobenzene, 4-nitroquinoline-1-oxide, and trans-4-phenyl-3-butene-2-one and peroxidase activity towards trans-2-nonenal and hexa-2,4-dienal. The FgGST1 was highly sensitive to inhibition by cibacron blue. The cofactor (GSH) and inhibitor (cibacron blue) were docked, and binding sites were identified. The molecular dynamics studies and principal component analysis indicated the stability of the systems and the collective motions, respectively. Unfolding studies suggest that FgGST1 is a highly cooperative molecule because, during GdnHCl-induced denaturation, a simultaneous unfolding of the protein without stabilization of any partially folded intermediate is observed. The protein is stabilized with a conformational free energy of about 10 ± 0.3 kcal mol−1. Additionally, the presence of conserved Pro-53 and structural motifs such as N-capping box and hydrophobic staple, further aided in the stability and proper folding of FgGST1.

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Structural insights into Charcot–Marie–Tooth disease‐linked mutations in human GDAP1

et al. 2022

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Charcot-Marie-Tooth disease (CMT) is the most common inherited peripheral polyneuropathy in humans, and its different subtypes are linked to mutations in dozens of different genes. Mutations in gangliosideinduced differentiation-associated protein 1 (GDAP1) cause two types of CMT, demyelinating CMT4A and axonal CMT2K. The GDAP1-linked CMT genotypes are mainly missense point mutations. Despite clinical profiling and in vivo studies on the mutations, the etiology of GDAP1-linked CMT is poorly understood. Here, we describe the biochemical and structural properties of the Finnish founding CMT2K mutation H123R and CMT2K-linked R120W, both of which are autosomal dominant mutations. The disease variant proteins retain close to normal structure and solution behavior, but both present a significant decrease in thermal stability. Using GDAP1 variant crystal structures, we identify a side-chain interaction network between helices ⍺3, ⍺6, and ⍺7, which is affected by CMT mutations, as well as a hinge in the long helix ⍺6, which is linked to structural flexibility. Structural analysis of GDAP1 indicates that CMT may arise from disruption of specific intra-and intermolecular interaction networks, leading to alterations in GDAP1 structure and stability, and, eventually, insufficient motor and sensory neuron function.Inherited polyneuropathies are a genetically and clinically diverse group of neurodegenerative diseases affecting motor and sensory neurons in the peripheral nervous system (PNS) [1,2]. Mutations in dozens of genes expressed in the PNS cause Charcot-Marie-Tooth disease (CMT). Based on clinical findings, CMT can be classified into three forms: demyelinating, axonal, and intermediate [3,4]. The progress of CMT is linked to the hereditary pattern, whereby the autosomal recessive form has an earlier onset and more severe symptoms than the autosomal dominant form [5][6][7]. Understanding the molecular function of the proteins involved in the etiology of neuropathies is vital in efforts toward treatment and diagnosis.

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Functional classification and biochemical characterization of a novel rho class glutathioneS‐transferase inSynechocystis PCC 6803

Cited by 18 publications

References 32 publications

Cytosolic Glutathione S-transferase in Bacteria: A Review

Cytosolic Glutathione S-transferase in Bacteria: A Review

Comprehensive analysis of the catalytic and structural properties of a mu-class glutathione s-transferase from Fasciola gigantica

Structural insights into Charcot–Marie–Tooth disease‐linked mutations in human GDAP1

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