Literature summary for 6.3.1.2 extracted from

Pantoja-Uceda, D.; Neira, J.L.; Saelices, L.; Robles-Rengel, R.; Florencio, F.J.; Muro-Pastor, M.I.; Santoro, J.
Dissecting the binding between glutamine synthetase and its two natively unfolded protein inhibitors (2016), Biochemistry, 55, 3370-3382 .

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Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	P77961	-	-

Synonyms

Synonyms	Comment	Organism
GS type I	-	Synechocystis sp. PCC 6803

General Information

General Information	Comment	Organism
physiological function	ammonium is incorporated into carbon skeletons by the sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) in cyanobacteria. The activity of Synechocystis sp. PCC 6803 GS type I enzyme is controlled by protein-protein interactions with two intrinsically disordered inactivating factors (IFs): the 65-residue (IF7) and the 149-residue one (IF17), NMR sequence analysis and structure study, overview. The electrostatic-determined binding does not follow a kinetic two-state model, the binding is not diffusion-limited	Synechocystis sp. PCC 6803

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Release 2023.1 (January 2023)