Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes

Autor: Guillermo Mulliert, Mathieu Schwartz, Thomas Roret, Claude Didierjean, Frédérique Favier, Aurélie Deroy, Thomas Perrot, Mélanie Morel-Rouhier, Eric Gelhaye
Přispěvatelé: Université de Lorraine (UL), Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Sorbonne Université (SU), Laboratory of Excellence Advanced Research on the Biology of Tree and Forest Ecosystems (ARBRE grant) ANR 11 LABX 0002 01, 'Impact Biomolecules' project of the 'Lorraine Universite d'Excellence' (Investissements d'avenir - ANR), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA)
Jazyk: angličtina
Rok vydání: 2018
Předmět:
0301 basic medicine
Models
Molecular
MECHANISM
dual enzyme activity
[SDV]Life Sciences [q-bio]
S-GLUTATHIONYL-(CHLORO)HYDROQUINONE REDUCTASES
Reductase
glutathionyl-hydroquinone reductase
Crystallography
X-Ray
Biochemistry
Substrate Specificity
POPULUS-TRICHOCARPA
trametes versicolor
Structural Biology
Transferase
HYDROQUINONE REDUCTASES
Phylogeny
Glutathione Transferase
Trametes
biology
Chemistry
glutathionyl-acetophenone reductase
glutathione transferase Xi
Glutathione
Isoenzymes
INSIGHTS
champignon ascomycete
gluthatione s transférase
Protein Binding
Gene isoform
GENES
Stereochemistry
Biophysics
Fungal Proteins
03 medical and health sciences
Residue (chemistry)
Protein Domains
Genetics
PLANTS
Amino Acid Sequence
Cysteine
crystallography
Molecular Biology
Gene
Trametes versicolor
Sequence Homology
Amino Acid
IDENTIFICATION
résidu cystéine
Active site
Cell Biology
S-TRANSFERASES
biology.organism_classification
REDUCTION
030104 developmental biology
champignon saprophyte
biology.protein
Biocatalysis
Zdroj: FEBS Letters
FEBS Letters, Wiley, 2018, 592 (18), pp.3163-3172. ⟨10.1002/1873-3468.13224⟩
ISSN: 0014-5793
1873-3468
DOI: 10.1002/1873-3468.13224⟩
Popis: Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quinones, Omega GSTs are specialized in the reduction of glutathionyl-acetophenones. Here, we present the biochemical and structural analysis of TvGSTX1 and TvGSTX3 isoforms from the wood-degrading fungus Trametes versicolor. TvGSTX1 reduces GS-menadione as expected, while TvGSTX3 reduces both Xi and Omega substrates. An in-depth structural analysis indicates a broader active site for TvGSTX3 due to specific differences in the nature of the residues situated in the C-terminal helix α9. This feature could explain the catalytic duality of TvGSTX3. Based on phylogenetic analysis, we propose that this duality might exist in saprophytic fungi and ascomycetes.
Databáze: OpenAIRE
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