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Literature summary for 2.5.1.18 extracted from

  • Caccuri, A.M.; Antonini, G.; Nicotra, M.; Battistoni, A.; Lo Bello, M.; Board, P.G.; Parker, M.W.; Ricci, G.
    Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina (1997), J. Biol. Chem., 272, 29681-29686.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Lucilia cuprina

Protein Variants

Protein Variants Comment Organism
S9A decreased kcat Lucilia cuprina
Y113F increased kcat Lucilia cuprina

Organism

Organism UniProt Comment Textmining
Lucilia cuprina
-
 sheep blowfly
-

Purification (Commentary)

Purification (Comment) Organism
-
 Lucilia cuprina

Reaction

Reaction Comment Organism Reaction ID
RX + glutathione = HX + R-S-glutathione mechanism Lucilia cuprina
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-chloro-2,4-dinitrobenzene + glutathione
-
 Lucilia cuprina S-(2,4-dinitrophenyl)-glutathione + HCl
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.28
-
 glutathione S9A mutant, cosubstrate: 1-chloro-2,4-dinitrobenzene Lucilia cuprina
53
-
 glutathione wild-type, cosubstrate: 1-chloro-2,4-dinitrobenzene Lucilia cuprina
144
-
 glutathione Y113F mutant, cosubstrate: 1-chloro-2,4-dinitrobenzene Lucilia cuprina