PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
17868038-2	2008	GMPS, a G-type amidotransferase, catalyses the amination of XMP to GMP with the reaction occurring in two domains, the GAT (glutamine amidotransferase) and ATPPase (ATP pyrophosphatase).	xanthosine monophosphate	60-63	guanine monophosphate synthase	Homo sapiens	0-4
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.	xanthosine monophosphate	154-157	guanine monophosphate synthase	Homo sapiens	62-66
15699053-2	2005	In rat brain extracts and in intact LoVo cells, xanthosine is salvaged to XMP via the phosphotransferase activity of cytosolic 5"-nucleotidase.	xanthosine monophosphate	74-77	5'-nucleotidase ecto	Homo sapiens	127-142
17324932-4	2007	Crystal structures of bifunctional ATIC in complex with nucleoside 2 and nucleotide 3 revealed IMPCH binding modes similar to that of the IMPCH feedback inhibitor, xanthosine 5"-monophosphate.	xanthosine monophosphate	164-191	5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase	Homo sapiens	35-39
15699053-6	2005	Thus, phosphorylation of xanthosine by cytosolic 5"-nucleotidase circumvents the activity of IMP dehydrogenase, a rate-limiting enzyme, catalyzing the NAD(+)-dependent conversion of IMP to XMP at the branch point of de novo nucleotide synthesis, thus leading to the generation of guanine nucleotides.	xanthosine monophosphate	189-192	5'-nucleotidase ecto	Homo sapiens	49-64
12501179-4	2002	Hence, the crystal structure of dimeric avian ATIC was determined as a complex with the AICAR Tfase substrate AICAR, as well as with an IMP cyclohydrolase inhibitor, XMP, to 1.93 A resolution.	xanthosine monophosphate	166-169	5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase	Homo sapiens	46-50
10758003-2	2000	Inosine 5"- monophosphate dehydrogenase (IMPDH) is the enzyme that catalyzes the oxidation of IMP to XMP with the concomitant reduction of nicotinamide adenine dinucleotide (from NAD(+) to NADH).	xanthosine monophosphate	101-104	inosine-5'-monophosphate dehydrogenase 2	Cricetulus griseus	41-46
10545171-1	1999	The crystal structure of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase (HGPRT)-xanthosine 5"-monophosphate (XMP)-pyrophosphate-Mg(2+) ternary complex has been determined at 1.	xanthosine monophosphate	102-129	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	95-100
10683258-1	2000	Inosine 5"-monophosphate dehydrogenase (IMPDH) catalyzes the oxidation of inosine 5"-monophosphate (IMP) to xanthosine 5"-monophosphate with the concomitant reduction of NAD to NADH.	xanthosine monophosphate	108-135	inosine-5'-monophosphate dehydrogenase 2	Cricetulus griseus	40-45
10545171-1	1999	The crystal structure of the Toxoplasma gondii hypoxanthine-guanine phosphoribosyltransferase (HGPRT)-xanthosine 5"-monophosphate (XMP)-pyrophosphate-Mg(2+) ternary complex has been determined at 1.	xanthosine monophosphate	131-134	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	95-100
1671845-1	1991	Inosinic acid (IMP) dehydrogenase (IMPD) catalyzes the conversion of IMP to XMP as the first committed step in GMP biosynthesis de novo.	xanthosine monophosphate	76-79	inosine monophosphate dehydrogenase 2	Mus musculus	35-39
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.	xanthosine monophosphate	83-110	guanine monophosphate synthase	Homo sapiens	0-14
7706277-13	1995	Interaction of GMP synthetase with xanthosine 5"-monophosphate (XMP), a substrate, exhibits sigmoidal kinetics with a Hill coefficient of 1.48 +/- 0.07.	xanthosine monophosphate	35-62	guanine monophosphate synthase	Homo sapiens	15-29
7706277-13	1995	Interaction of GMP synthetase with xanthosine 5"-monophosphate (XMP), a substrate, exhibits sigmoidal kinetics with a Hill coefficient of 1.48 +/- 0.07.	xanthosine monophosphate	64-67	guanine monophosphate synthase	Homo sapiens	15-29
7706277-14	1995	This positive cooperativity is not due to ligand-induced oligomerization, since GMP synthetase remains a monomer in the presence of XMP and other substrates.	xanthosine monophosphate	132-135	guanine monophosphate synthase	Homo sapiens	80-94
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.	xanthosine monophosphate	150-153	guanine monophosphate synthase	Homo sapiens	37-51
1761576-4	1991	Subsequent genetic and biochemical analyses identified a p53 induction-related purine pathway defect which was localized to the step of inosine 5"-monophosphate conversion to xanthosine 5"-monophosphate.	xanthosine monophosphate	175-202	transformation related protein 53, pseudogene	Mus musculus	57-60
29042184-5	2018	The majority of nucleotide ligands bind selectively at one of the two active sites with the exception of xanthosine monophosphate, XMP, which, in addition to binding in both AICARFT and IMPCH active sites, shows evidence for cooperative binding with communication between symmetrically-related active sites in the two IMPCH domains.	xanthosine monophosphate	131-134	5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase	Homo sapiens	174-181
35102890-8	2022	Analysis of the substrate-binding pockets of A. fumigatus GMP synthase reveals key differences in the ATP- and XMP-binding sites that can be exploited for species-specific inhibitor drug design.	xanthosine monophosphate	111-114	guanine monophosphate synthase	Homo sapiens	58-70
2789248-1	1989	The endocytosis of Ag mediated by membrane-associated Ig (mIg) molecules has been spectrophotometrically monitored using a cell line (2C3) specific for the hapten phthalate (Xmp) and employing conjugates of Xmp and horseradish peroxidase (HRP) as the labeled ligand.	xanthosine monophosphate	174-177	chemokine (C-X-C motif) ligand 9	Mus musculus	54-56
2789248-1	1989	The endocytosis of Ag mediated by membrane-associated Ig (mIg) molecules has been spectrophotometrically monitored using a cell line (2C3) specific for the hapten phthalate (Xmp) and employing conjugates of Xmp and horseradish peroxidase (HRP) as the labeled ligand.	xanthosine monophosphate	174-177	chemokine (C-X-C motif) ligand 9	Mus musculus	58-61
2789248-1	1989	The endocytosis of Ag mediated by membrane-associated Ig (mIg) molecules has been spectrophotometrically monitored using a cell line (2C3) specific for the hapten phthalate (Xmp) and employing conjugates of Xmp and horseradish peroxidase (HRP) as the labeled ligand.	xanthosine monophosphate	207-210	chemokine (C-X-C motif) ligand 9	Mus musculus	54-56
2789248-1	1989	The endocytosis of Ag mediated by membrane-associated Ig (mIg) molecules has been spectrophotometrically monitored using a cell line (2C3) specific for the hapten phthalate (Xmp) and employing conjugates of Xmp and horseradish peroxidase (HRP) as the labeled ligand.	xanthosine monophosphate	207-210	chemokine (C-X-C motif) ligand 9	Mus musculus	58-61
2822457-5	1987	dNase activity occurred with both purine and pyrimidine substrates and was maximal with deoxy analogs (dIMP much greater than dUMP greater than dGMP greater than dTMP = dAMP much greater than dCMP) at a pH optimum of 6.2, but slight cross-reactivity occurred with some nondeoxy substrates (IMP greater than GMP greater than UMP = XMP greater than CMP).	xanthosine monophosphate	330-333	Deoxyribonuclease II	Drosophila melanogaster	0-5
26756917-1	2016	Human Guanine Monophosphate Synthetase (hGMPS) converts XMP to GMP, and acts as a bifunctional enzyme with N-terminal "glutaminase" (GAT) and C-terminal "synthetase" domain.	xanthosine monophosphate	56-59	guanine monophosphate synthase	Homo sapiens	6-38
26756917-1	2016	Human Guanine Monophosphate Synthetase (hGMPS) converts XMP to GMP, and acts as a bifunctional enzyme with N-terminal "glutaminase" (GAT) and C-terminal "synthetase" domain.	xanthosine monophosphate	56-59	guanine monophosphate synthase	Homo sapiens	40-45
26043892-2	2015	The purine salvage pathway is redundant and contains two routes to guanosine-5"-monophosphate (GMP) formation: conversion from xanthosine-5"-monophosphate (XMP) by GMP synthase (GMPS) or direct salvage of guanine by hypoxanthine-guanine phosphoribosyltransferase (HGPRT).	xanthosine monophosphate	127-154	guanine monophosphate synthetase	Mus musculus	178-182
26043892-2	2015	The purine salvage pathway is redundant and contains two routes to guanosine-5"-monophosphate (GMP) formation: conversion from xanthosine-5"-monophosphate (XMP) by GMP synthase (GMPS) or direct salvage of guanine by hypoxanthine-guanine phosphoribosyltransferase (HGPRT).	xanthosine monophosphate	156-159	guanine monophosphate synthetase	Mus musculus	178-182
25869206-4	2015	In this study, we report that in PCa cells de novo purine biosynthesis and the subsequent conversion to XMP is tightly regulated by MYC and independent of AR activity.	xanthosine monophosphate	104-107	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	132-135
23816837-5	2013	Substrate XMP was bound in the crystal structure of the human GMPS enzyme.	xanthosine monophosphate	10-13	guanine monophosphate synthase	Homo sapiens	62-66
23841499-3	2013	Guanosine 5"-monophosphate synthetase (GMPS) is one of three glutamine amidotransferases in de novo purine biosynthesis and is responsible for the last step in the guanosine branch of the pathway, the amination of xanthosine 5"-monophosphate (XMP).	xanthosine monophosphate	214-241	guanine monophosphate synthase	Homo sapiens	0-37
23841499-3	2013	Guanosine 5"-monophosphate synthetase (GMPS) is one of three glutamine amidotransferases in de novo purine biosynthesis and is responsible for the last step in the guanosine branch of the pathway, the amination of xanthosine 5"-monophosphate (XMP).	xanthosine monophosphate	214-241	guanine monophosphate synthase	Homo sapiens	39-43
23841499-3	2013	Guanosine 5"-monophosphate synthetase (GMPS) is one of three glutamine amidotransferases in de novo purine biosynthesis and is responsible for the last step in the guanosine branch of the pathway, the amination of xanthosine 5"-monophosphate (XMP).	xanthosine monophosphate	243-246	guanine monophosphate synthase	Homo sapiens	0-37
23841499-3	2013	Guanosine 5"-monophosphate synthetase (GMPS) is one of three glutamine amidotransferases in de novo purine biosynthesis and is responsible for the last step in the guanosine branch of the pathway, the amination of xanthosine 5"-monophosphate (XMP).	xanthosine monophosphate	243-246	guanine monophosphate synthase	Homo sapiens	39-43
22119138-2	2012	The conversion of XMP to GMP is catalyzed by guaA-encoded GMP synthetase (GMPS), and deletions in the Shiguella flexneri guaBA operon led to an attenuated auxotrophic strain.	xanthosine monophosphate	18-21	GMP synthase	Mycobacterium tuberculosis H37Rv	45-49
21486037-0	2011	Hypoxanthine guanine phosphoribosyltransferase distorts the purine ring of nucleotide substrates and perturbs the pKa of bound xanthosine monophosphate.	xanthosine monophosphate	127-151	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	0-46
21486037-7	2011	We used ultraviolet resonance Raman spectroscopy to study the complexes of HGPRT with products (IMP, GMP, and XMP), in both organisms, in resonance with the purine nucleobase electronic absorption.	xanthosine monophosphate	110-113	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	75-80
21486037-12	2011	While hHGPRT does not bind XMP, PfHGPRT perturbs the pK(a) of bound XMP.	xanthosine monophosphate	68-71	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	6-12
19900465-7	2010	We have also demonstrated that PH-GATase (the glutamine amidotransferase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon P. horikoshii OT3) alone is inactive, and that all substrates of PH-ATPPase except for ammonia (Mg(2+), ATP and XMP) are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits.	xanthosine monophosphate	258-261	type 1 glutamine amidotransferase	Pyrococcus horikoshii OT3	34-40
19900465-7	2010	We have also demonstrated that PH-GATase (the glutamine amidotransferase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon P. horikoshii OT3) alone is inactive, and that all substrates of PH-ATPPase except for ammonia (Mg(2+), ATP and XMP) are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits.	xanthosine monophosphate	258-261	type 1 glutamine amidotransferase	Pyrococcus horikoshii OT3	46-72