Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.18 extracted from

  • Ricci, G.; Caccuri, A.M.; Lo Bello, M.; Rosato, N.; Mei, G.; Nicotra, M.; Chiessi, E.; Mazzetti, A.P.; Federici, G.
    Structural flexibility modulates the activity of human glutathione transferase P1-1. Role of helix 2 flexibility in the catalytic mechanism (1996), J. Biol. Chem., 271, 16187-16192.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
C47S decreased kcat Homo sapiens
C47S/C101S decreased kcat Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
transferase P1-1
-

Purification (Commentary)

Purification (Comment) Organism
isoenzyme P1-1 Homo sapiens

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 + 1-fluoro-2,4-dinitrobenzene
-
Homo sapiens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
76
-
1-chloro-2,4-dinitrobenzene
-
Homo sapiens
106
-
1-Fluoro-2,4-dinitrobenzene
-
Homo sapiens