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Literature summary for 2.5.1.18 extracted from

  • Caccuri, A.M.; Ascenzi, P.; Antonini, G.; Parker, M.W.; Oakley, A.J.; Chiessi, E.; Nuccetelli, M.; Battistoni, A.; Bellizia, A.; Ricci, G.
    Structural flexibility modulates the activity of human glutathione transferase P1-1. Influence of a poor co-substrate on dynamics and kinetics of human glutathione transferase (1996), J. Biol. Chem., 271, 16193-16198.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
C47S
-
 Homo sapiens
C47S/C101S
-
 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
S-(2,4-dinitrophenyl)glutathione product inhibition Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild type and mutants Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
RX + glutathione = HX + R-S-glutathione kinetic mechanism Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
placenta
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 1-chloro-2,4-dinitrobenzene
-
 Homo sapiens S-2,4-dinitrophenylglutathione + HCl
-
 ?
glutathione + 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole poor substrate Homo sapiens ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
761
-
 1-chloro-2,4-dinitrobenzene transferase P1-1, cofactor: glutathione Homo sapiens