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Literature summary for 2.5.1.18 extracted from

  • Stockman, P.K.; McLellan, L.I.; Hayes, J.D.
    Characterization of the basic glutathione S-transferase B1 and B2 subunits from human liver (1987), Biochem. J., 244, 55-61.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.18

Inhibitors

Inhibitors Comment Organism Structure
bromosulfophthalein
-
 Homo sapiens
Hematin
-
 Homo sapiens
Tributyltin acetate
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
80 272 with 1-chloro-2,4-dinitrobenzene as substrate Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + 1,2-dichloro-4-nitrobenzene
-
 Homo sapiens ?
-
 ?
glutathione + 1-chloro-2,4-dinitrobenzene
-
 Homo sapiens S-2,4-dinitrophenylglutathione + HCl
-
 ?
glutathione + cumene hydroperoxide
-
 Homo sapiens ?
-
 ?
glutathione + trans-4-phenyl-3-buten-2-one
-
 Homo sapiens ?
-
 ?
additional information specificity Homo sapiens ?
-
 ?
additional information enzyme has also selenium-independent peroxidase activity Homo sapiens ?
-
 ?
RX + glutathione RX: R: aliphatic, aromatic or heterocyclic, X: sulfate, nitrite or halide, enzyme also catalyzes: the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrite, certain isomerization reactions and disulfide interchange Homo sapiens HX + R-S-glutathione
-
 ?

Subunits

Subunits Comment Organism
dimer dimeric forms: B1B1, B2B2 and B1B2 Homo sapiens