Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.5.1.18	-	Homo sapiens

Protein Variants

EC Number	Protein Variants	Comment	Organism
2.5.1.18	C47S	decreased kcat	Homo sapiens
2.5.1.18	C47S/C101S	decreased kcat	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.5.1.18	Homo sapiens	-	transferase P1-1	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.5.1.18	isoenzyme P1-1	Homo sapiens

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.5.1.18	placenta	-	Homo sapiens	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.5.1.18	glutathione + 1-chloro-2,4-dinitrobenzene	-	Homo sapiens	S-2,4-dinitrophenylglutathione + HCl	-	?
2.5.1.18	glutathione + 1-fluoro-2,4-dinitrobenzene	-	Homo sapiens	?	-	?

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.5.1.18	76	-	1-chloro-2,4-dinitrobenzene	-	Homo sapiens
2.5.1.18	106	-	1-Fluoro-2,4-dinitrobenzene	-	Homo sapiens

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Release 2023.1 (January 2023)