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Literature summary for 2.5.1.18 extracted from

  • Fabrini, R.; Bocedi, A.; Dawood, K.F.; Turella, P.; Stella, L.; Parker, M.W.; Pedersen, J.Z.; Federici, G.; Antonini, G.; Ricci, G.
    The extended catalysis of glutathione transferase (2011), FEBS Lett., 585, 341-345.
    View publication on PubMed
Search for more literature for 2.5.1.18

Activating Compound

Activating Compound Comment Organism Structure
iodoacetic acid
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information pseudo-first order kinetic constants, simplified Michaelis-Menten steady-state model for simulation of the overall dependence of the rate of product formationon either substrate or enzyme concentrations, with substrate 1-chloro-2,4-dinitrobenzene Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus glutathione transferases from rat liver are able to conjugate GSH to many hydrophobic toxic compounds. Small and hydrophilic disulfides like cystine, cystamine and dithioethanol, and hydrophilic alkylating compounds like iodoacetate, are no substrates of this enzyme. Omega class GST and a peculiar lens GST display a moderate thiol transferase activity with dithioethanol ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
hepatocyte
-
 Rattus norvegicus
-
lens
-
 Rattus norvegicus
-
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-chloro-2,4-dinitrobenzene + glutathione
-
 Rattus norvegicus S-(2,4-dinitrophenyl)glutathione + HCl
-
 ?
additional information glutathione transferases from rat liver are able to conjugate GSH to many hydrophobic toxic compounds. Small and hydrophilic disulfides like cystine, cystamine and dithioethanol, and hydrophilic alkylating compounds like iodoacetate, are no substrates of this enzyme. Omega class GST and a peculiar lens GST display a moderate thiol transferase activity with dithioethanol Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
alpha GST
-
 Rattus norvegicus
GST
-
 Rattus norvegicus
Mu GST
-
 Rattus norvegicus
Omega class GST
-
 Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7.1 assay at Rattus norvegicus