PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
22060122-3	2011	PG catalyzed incorporation of (15)N-labeled ammonium ions into reactive glutamine amide groups in alpha-lactalbumin similarly to TGase and deamidated the most reactive glutamine amide group once labeled with (15)N. Furthermore, we investigated the effect of ammonium ions on the PG activity by peptide mapping, and more reactive glutamine residues were detected than were detected by the ELT in the presence of ammonium ions.	Glutamamide	72-87	lactalbumin alpha	Homo sapiens	98-115
14515209-1	2003	Human proinsulin C-peptide with C-terminal glutamine amide could be prepared through solid phase method by combining the gamma-carboxyl group of glutamic acid with the amino group of MBHA resin.	Glutamamide	43-58	insulin	Homo sapiens	6-16
9485308-5	1998	Thus, FMN is the flavin located at the site of reduction of the iminoglutarate formed on the addition of glutamine amide group to the C(2) carbon of 2-oxoglutarate.	Glutamamide	105-120	formin 1	Homo sapiens	6-9
33768538-2	2021	Guanosine monophosphate synthetase (GMPS) acts in the de novo purine biosynthesis pathway, utilizing a glutamine amide to synthesize the guanine nucleotide.	Glutamamide	103-118	guanine monophosphate synthase	Homo sapiens	0-34
33768538-2	2021	Guanosine monophosphate synthetase (GMPS) acts in the de novo purine biosynthesis pathway, utilizing a glutamine amide to synthesize the guanine nucleotide.	Glutamamide	103-118	guanine monophosphate synthase	Homo sapiens	36-40
2674138-1	1989	A family of four glutamine amidotransferases has a homologous glutamine amide transfer domain, designated purF-type, that is named after purF-encoded glutamine phosphoribosylpyrophosphate amidotransferase.	Glutamamide	62-77	phosphoribosyl pyrophosphate amidotransferase	Homo sapiens	150-204
2674138-3	1989	Site-directed mutagenesis was used to replace several of the 9 invariant amino acids in the glutamine amide transfer domain of glutamine phosphoribosylpyrophosphate amidotransferase.	Glutamamide	92-107	phosphoribosyl pyrophosphate amidotransferase	Homo sapiens	127-181
2674138-4	1989	The results indicate that a Cys1-His101-Asp29 catalytic triad is involved in the glutamine amide transfer function of this enzyme.	Glutamamide	81-96	cystin 1	Homo sapiens	28-32
11842094-2	2002	A member of the N-terminal nucleophile class of amidotransferases, GFAT transfers the amino group from the L-glutamine amide to D-fructose 6-phosphate, producing glutamic acid and glucosamine 6-phosphate.	Glutamamide	107-124	glutamine--fructose-6-phosphate transaminase 1	Homo sapiens	67-71