Literature summary extracted from

Chang, L.
The functional involvement of Lys-38 in the heavy subunit of rat kidney gamma-glutamylcysteine synthetase: chemical modification and mutagenesis studies (1996), J. Protein Chem., 15, 321-326.

Protein Variants

EC Number	Protein Variants	Comment	Organism
6.3.2.2	K38A	mutant enzyme Lys38Arg: small changes in the catalytic properties, mutant enzyme K38N and K38E show marked decrease in enzymatic activity and about 2fold increase in Km for Glu	Rattus norvegicus

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
6.3.2.2	Trinitrobenzene sulfonate	addition of 10 mM Mg2+ results in a 16fold increase of inactivation rate, Lys-38 in the heavy subunit is significantly modified in presence of Mg2+	Rattus norvegicus

Organism

EC Number	Organism	UniProt	Comment	Textmining
6.3.2.2	Rattus norvegicus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
6.3.2.2	kidney	-	Rattus norvegicus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
6.3.2.2	ATP + L-Glu + L-Cys	-	Rattus norvegicus	ADP + phosphate + gamma-L-Glu-L-Cys	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)