Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics

Valenzuela-Chavira, Ignacio; Contreras-Vergara, Carmen A.; Arvizu‐Flores, Aldo A.; Serrano‐Posada, Hugo; López-Zavala, Alonso A.; García-Orozco, Karina D.; Hernández-Paredes, Javier; Rudino‐Pinera, E.; Stojanoff, V.; Sotelo‐Mundo, Rogerio R.; Islas-Osuna, María A.

doi:10.1016/j.biochi.2017.01.005

Cited by 19 publications

(13 citation statements)

References 62 publications

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“…Within a class, the variable regions are often close to the active site and involved in the binding of the electrophilic substrate. In GSTUs, these regions include helix α9 and the segment from roughly the C-terminal end of α4 to the N-terminal end of α5 (Valenzuela-Chavira et al, 2017). In GSTFs, they include this segment and the connection β2-β3, which, in maize GSTF3, was supposed to move upon binding of the substrate in the active site (Neuefeind et al, 1997a).…”

Section: Introductionmentioning

confidence: 99%

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases

et al. 2019

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Glutathione transferases (GSTs) belong to a ubiquitous multigenic family of enzymes involved in diverse biological processes including xenobiotic detoxification and secondary metabolism. A canonical GST is formed by two domains, the N-terminal one adopting a thioredoxin (TRX) fold and the C-terminal one an all-helical structure. The most recent genomic and phylogenetic analysis based on this domain organization allowed the classification of the GST family into 14 classes in terrestrial plants. These GSTs are further distinguished based on the presence of the ancestral cysteine (Cys-GSTs) present in TRX family proteins or on its substitution by a serine (Ser-GSTs). Cys-GSTs catalyze the reduction of dehydroascorbate and deglutathionylation reactions whereas Ser-GSTs catalyze glutathione conjugation reactions and eventually have peroxidase activity, both activities being important for stress tolerance or herbicide detoxification. Through non-catalytic, so-called ligandin properties, numerous plant GSTs also participate in the binding and transport of small heterocyclic ligands such as flavonoids including anthocyanins, and polyphenols. So far, this function has likely been underestimated compared to the other documented roles of GSTs. In this review, we compiled data concerning the known enzymatic and structural properties as well as the biochemical and physiological functions associated to plant GSTs having a conserved serine in their active site.

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Section: Introductionmentioning

confidence: 99%

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases

et al. 2019

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“…By deprotonating the thiol, activating GSH carries out nucleophilic attack on the electrophilic center of hydrophobic substrate to detoxicate aryl halides or to act as an electron donor to reduce peroxides [29]. Although the topology and polypeptide sequences involved are quite diverse, the H-site is composed predominantly of hydrophobic residues, which enable a wide range of hydrophobic substrates to identify the H-site accurately in the polar cavity [30]. Compared with the highly conserved G-site, the structural variability at the H-site is more important for the catalytic mechanism.…”

Section: Introductionmentioning

confidence: 99%

Effects of Substrate-Binding Site Residues on the Biochemical Properties of a Tau Class Glutathione S-Transferase from Oryza sativa

Yang

Wei

et al. 2019

Genes

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Glutathione S-transferases (GSTs)—an especially plant-specific tau class of GSTs—are key enzymes involved in biotic and abiotic stress responses. To improve the stress resistance of crops via the genetic modification of GSTs, we predicted the amino acids present in the GSH binding site (G-site) and hydrophobic substrate-binding site (H-site) of OsGSTU17, a tau class GST in rice. We then examined the enzyme activity, substrate specificity, enzyme kinetics and thermodynamic stability of the mutant enzymes. Our results showed that the hydrogen bonds between Lys42, Val56, Glu68, and Ser69 of the G-site and glutathione were essential for enzyme activity and thermal stability. The hydrophobic side chains of amino acids of the H-site contributed to enzyme activity toward 4-nitrobenzyl chloride but had an inhibitory effect on enzyme activity toward 1-chloro-2,4-dinitrobenzene and cumene hydroperoxide. Different amino acids of the H-site had different effects on enzyme activity toward a different substrate, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Moreover, Leu112 and Phe162 were found to inhibit the catalytic efficiency of OsGSTU17 to 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, while Pro16, Leu112, and Trp165 contributed to structural stability. The results of this research enhance the understanding of the relationship between the structure and function of tau class GSTs to improve the abiotic stress resistance of crops.

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“…Other polar contacts with the tripeptide include residues K42 (loop β 2 -α 2 ), I56 (loop α 2 -β 3 ), E68 and S69 (helix α 3 ) (PDB 1OYJ, OsGSTU1 numbering). Concerning the H-site, studies have pointed to residues located in the vicinity of the conserved serine, in loop β 1 -α 1 , helix α 4 , helix α 6 and helix α 9 [64][65][66][67][68]. A third site called the ligandin site was reported for Glycine max GSTU4-4 which binds one (4-nitrophenyl)methanethiol molecule in a hydrophobic region made of residues from helix α 1 , strand β 2 and helix α 8 [66].…”

Section: (B) Modelling Of Protoporphyrin/haem Binding By Tau Glutathione Transferasesmentioning

confidence: 99%

Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?

Sylvestre-Gonon

Schwartz

Girardet

et al. 2020

Phil. Trans. R. Soc. B

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In plants, tetrapyrrole biosynthesis occurs in chloroplasts, the reactions being catalysed by stromal and membrane-bound enzymes. The tetrapyrrole moiety is a backbone for chlorophylls and cofactors such as sirohaems, haems and phytochromobilins. Owing to this diversity, the potential cytotoxicity of some precursors and the associated synthesis costs, a tight control exists to adjust the demand and the fluxes for each molecule. After synthesis, haems and phytochromobilins are incorporated into proteins found in other subcellular compartments. However, there is only very limited information about the chaperones and membrane transporters involved in the trafficking of these molecules. After summarizing evidence indicating that glutathione transferases (GST) may be part of the transport and/or degradation processes of porphyrin derivatives, we provide experimental data indicating that tau glutathione transferases (GSTU) bind protoporphyrin IX and haem moieties and use structural modelling to identify possible residues responsible for their binding in the active site hydrophobic pocket. Finally, we discuss the possible roles associated with the binding, catalytic transformation (i.e. glutathione conjugation) and/or transport of tetrapyrroles by GSTUs, considering their subcellular localization and capacity to interact with ABC transporters. This article is part of the theme issue ‘Retrograde signalling from endosymbiotic organelles’.

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Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics

Cited by 19 publications

References 62 publications

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases

Functional, Structural and Biochemical Features of Plant Serinyl-Glutathione Transferases

Effects of Substrate-Binding Site Residues on the Biochemical Properties of a Tau Class Glutathione S-Transferase from Oryza sativa

Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants?

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