Literature summary for 4.3.2.10 extracted from

Rivalta, I.; Lisi, G.P.; Snoeberger, N.S.; Manley, G.; Loria, J.P.; Batista, V.S.
Allosteric communication disrupted by a small molecule binding to the imidazole glycerol phosphate synthase protein-protein interface (2016), Biochemistry, 55, 6484-6494 .

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Application

Application	Comment	Organism
agriculture	development of allosteric antibiotics, herbicides, and antifungal compounds because the enzyme is absent in mammals but provides an entry point to fundamental biosynthetic pathways in plants, fungi, and bacteria	Thermotoga maritima
pharmacology	development of allosteric antibiotics, herbicides, and antifungal compounds because the enzyme is absent in mammals but provides an entry point to fundamental biosynthetic pathways in plants, fungi, and bacteria	Thermotoga maritima

Inhibitors

Inhibitors	Comment	Organism	Structure
7-benzyl-8-[(1-[[(2-hydroxyethyl)amino]methyl]propyl)amino]-1,3-dimethyl-2,3,6,7-tetrahydro-1H-2,6-purinedione	glutaminase activity is substantially suppressed upon binding of the inhibitor to the HisH-HisF interface. The allosteric inhibitor is able to uncouple motions induced by the effector ligand with essential motions in the distant active site, favoring an inactive conformation of this V-type enzyme	Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9X0C8 and Q9X0C6	Q9X0C8: subunit HisH, Q9X0C6: subunit HisF	-
Thermotoga maritima ATCC 43589	Q9X0C8 and Q9X0C6	Q9X0C8: subunit HisH, Q9X0C6: subunit HisF	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamine + H2O	-	Thermotoga maritima	L-glutamate + NH3	-	?
L-glutamine + H2O	-	Thermotoga maritima ATCC 43589	L-glutamate + NH3	-	?

Synonyms

Synonyms	Comment	Organism
IGPS	-	Thermotoga maritima

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Release 2023.1 (January 2023)