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Literature summary for 2.5.1.18 extracted from

  • Vander Jagt, D.L.; Hunsaker, L.A.; Garcia, K.B.; Royer, R.E.
    Isolation and characterization of the multiple glutathione S-transferases from human liver. Evidence for unique heme-binding sites (1985), J. Biol. Chem., 260, 11603-11610.
    View publication on PubMed
Search for more literature for 2.5.1.18

Inhibitors

Inhibitors Comment Organism Structure
bilirubin 50% inhibition at 0.01-0.02 mM Homo sapiens
Hematin non competitive with transferase activity Homo sapiens
N-ethylmaleimide completely inhibits form IX and X at 20 mM after 30 min, but not forms I-VIII Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25200
-
 2 * 25200, form I-XII, SDS-PAGE Homo sapiens
25600
-
 2 * 25600, form XIII, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 13 forms
-

Purification (Commentary)

Purification (Comment) Organism
13 isoforms Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-
liver
-
 Homo sapiens
-
placenta
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5 8.3 with cumene hydroperoxide as substrate Homo sapiens
33 94 with 1-chloro-2,4-dinitrobenzene as substrate Homo sapiens
104
-
-
 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 + cumene hydroperoxide
-
 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 2 * 25600, form XIII, SDS-PAGE Homo sapiens
dimer 2 * 25200, form I-XII, SDS-PAGE Homo sapiens