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Literature summary for 2.5.1.18 extracted from

  • Fyfe, P.K.; Westrop, G.D.; Silva, A.M.; Coombs, G.H.; Hunter, W.N.
    Leishmania TDR1 structure, a unique trimeric glutathione transferase capable of deglutathionylation and antimonial prodrug activation (2012), Proc. Natl. Acad. Sci. USA, 109, 11693-11698.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.18

Crystallization (Commentary)

Crystallization (Comment) Organism
SeMet TDR1 in complex with glutathione, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 2.3 a resolution, single-wavelength anomalous diffraction, modeling Leishmania infantum

Organism

Organism UniProt Comment Textmining
Leishmania infantum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-chloro-2,4-dinitrobenzene + glutathione
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 Leishmania infantum S-(2,4-dinitrophenyl)glutathione + HCl
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 ?
2-hydroxyethyl disulfide + glutathione
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 Leishmania infantum ?
-
 ?
additional information TDR1 displays weak GSTactivity with 1-chloro-2,4-dinitrobenzene, and a glutaredoxin-like thioltransferase activity, with hydroxyethyl disulfide, together with a previously noted dihydroascorbate reductase activity. The peptide substrate SQLWCLSN, with a bulky tryptophan adjacent to the cysteine, may not be optimal for binding to the sterically restricted G-I site on TDR1 leading to low deglutathionylation activity Leishmania infantum ?
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 ?

Subunits

Subunits Comment Organism
trimer structure of TDR1 reveals a unique trimer of subunits each containing two glutathione-S-transferase domains. The TDR1 subunit is constructed from two GST-like domains with a short linker region. The domains themselves consist of N-terminal glutaredoxin-like and C-terminal alpha-helical subdomains Leishmania infantum

Synonyms

Synonyms Comment Organism
glutathione-S-transferase
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 Leishmania infantum
GST
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 Leishmania infantum
TDR1
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 Leishmania infantum
thiol-dependent reductase I
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 Leishmania infantum

General Information

General Information Comment Organism
evolution TDR1 belongs to the glutathione-S-transferase (GST) superfamily Leishmania infantum
physiological function posttranslational S-glutathionylation modifications and glutaredoxin-dependent deglutathionylation participate in the regulation of metabolism and redox signalling in most organisms. Thiol-dependent reductase I, TDR1, an enzyme found in parasitic Leishmania species and Trypanosoma cruzi, is implicated in deglutathionylation and activation of antimonial prodrugs used to treat leishmaniasis. The deglutathionylation activity of TDR1 implies that glutathione itself has regulatory intracellular roles in addition to being a precursor for trypanothione, the major low mass thiol present in trypanosomatids Leishmania infantum