PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7706277-15	1995	Decoyinine, a selective inhibitor of GMP synthetase, inhibits the human enzyme reversibly with uncompetitive inhibition kinetics toward glutamine and XMP and non-competitive kinetics toward ATP.	Glutamine	136-145	guanine monophosphate synthase	Homo sapiens	37-51	
7559506-0	1995	The glutamine hydrolysis function of human GMP synthetase.	Glutamine	4-13	guanine monophosphate synthase	Homo sapiens	43-57	
7559506-2	1995	GMP synthetase (EC 6.3.5.2) is an amidotransferase that catalyzes the amination of xanthosine 5"-monophosphate to form GMP in the presence of glutamine and ATP.	Glutamine	142-151	guanine monophosphate synthase	Homo sapiens	0-14	
33768538-0	2021	Inhibition of guanosine monophosphate synthetase (GMPS) blocks glutamine metabolism and prostate cancer growth.	Glutamine	63-72	guanine monophosphate synthase	Homo sapiens	14-48	
33768538-0	2021	Inhibition of guanosine monophosphate synthetase (GMPS) blocks glutamine metabolism and prostate cancer growth.	Glutamine	63-72	guanine monophosphate synthase	Homo sapiens	50-54	
35102890-9	2022	Furthermore, the inhibitory activities of the glutamine analogues acivicin (IC50 = 16.6 +- 2.4 microM) and 6-diazo-5-oxo-L-norleucine (IC50 = 29.6 +- 5.6 microM) against A. fumigatus GMP synthase are demonstrated.	Glutamine	46-55	guanine monophosphate synthase	Homo sapiens	183-195	
3902841-2	1985	Conserved amino acid residues likely to be essential for glutamine-dependent activity were identified by alignment of the glutamine amide transfer domains in four different enzymes: anthranilate synthase component II (AS II), p-aminobenzoate synthase component II, GMP synthetase, and carbamoyl-P synthetase.	Glutamine	57-66	guanine monophosphate synthase	Homo sapiens	265-279	
4531004-0	1974	Glutamine-binding subunit of glutamate synthase and partial reactions catalyzed by this glutamine amidotransferase.	Glutamine	0-9	guanine monophosphate synthase	Homo sapiens	88-114	
23841499-4	2013	In several amidotransferases, the intramolecular path of ammonia from glutamine to substrate is understood; however, the crystal structure of GMPS only hinted at the details of such transfer.	Glutamine	70-79	guanine monophosphate synthase	Homo sapiens	142-146	
17868038-5	2008	Our studies aimed at understanding the kinetic mechanism of PfGMPS (Plasmodium falciparum GMPS) indicated steady-state ordered binding of ATP followed by XMP to the ATPPase domain with glutamine binding in a random manner to the GAT domain.	Glutamine	185-194	guanine monophosphate synthase	Homo sapiens	62-66