Literature summary for 6.3.1.2 extracted from

Sun, Y.; Ou, Y.; Cheng, M.; Ruan, Y.; van der Hoorn, F.A.
Binding of nickel to testicular glutamate-ammonia ligase inhibits its enzymatic activity (2011), Mol. Reprod. Dev., 78, 104-115.

Search for more literature for 6.3.1.2

Cloned(Commentary)

Cloned (Comment)	Organism
-	Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism	Structure
Ni2+	higher affinity for nickel than for the regular co-factor manganese. Upon binding, nickel interferes with the manganese-catalyzed enzymatic activity of recombinant GLUL protein. GLUL activity in testes of animals exposed to nickel sulfate is reduced	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	required, optimum concentration around 0.5 mM	Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
42000	-	x * 42000, SDS-PAGE	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
testis	predominantly in interstitial cell	Rattus norvegicus	-

Subunits

Subunits	Comment	Organism
?	x * 42000, SDS-PAGE	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
GLUL	-	Rattus norvegicus

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.2	-	pH 6.2, 37°C	Rattus norvegicus	Ni2+

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)