PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
9030564-2	1997	The monooxygenase, PAM, first catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine derivative, and the lyase, PGL, then catalyzes breakdown of this alpha-hydroxyglycine derivative to the amidated peptide plus glyoxylate.	aminohydroxyacetic acid	106-126	peptidylglycine alpha-amidating monooxygenase L homeolog	Xenopus laevis	19-22
9030564-2	1997	The monooxygenase, PAM, first catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine derivative, and the lyase, PGL, then catalyzes breakdown of this alpha-hydroxyglycine derivative to the amidated peptide plus glyoxylate.	aminohydroxyacetic acid	192-212	peptidylglycine alpha-amidating monooxygenase L homeolog	Xenopus laevis	19-22
7493955-2	1995	The monooxygenase, PAM, first catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine derivative, and the lyase, PGL, then catalyzes breakdown of this alpha-hydroxyglycine derivative to the amidated peptide plus glyoxylate.	aminohydroxyacetic acid	106-126	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	19-22
7493955-2	1995	The monooxygenase, PAM, first catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine derivative, and the lyase, PGL, then catalyzes breakdown of this alpha-hydroxyglycine derivative to the amidated peptide plus glyoxylate.	aminohydroxyacetic acid	106-126	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	154-157
7493955-2	1995	The monooxygenase, PAM, first catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine derivative, and the lyase, PGL, then catalyzes breakdown of this alpha-hydroxyglycine derivative to the amidated peptide plus glyoxylate.	aminohydroxyacetic acid	192-212	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	19-22
7493955-2	1995	The monooxygenase, PAM, first catalyzes conversion of a glycine-extended pro-peptide to the corresponding alpha-hydroxyglycine derivative, and the lyase, PGL, then catalyzes breakdown of this alpha-hydroxyglycine derivative to the amidated peptide plus glyoxylate.	aminohydroxyacetic acid	192-212	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	154-157
7493955-3	1995	We have previously established that PAM and PGL exhibit tandem reaction stereospecificities, with PAM producing, and PGL being reactive toward, only alpha-hydroxyglycine derivatives of absolute configuration (S).	aminohydroxyacetic acid	149-169	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	36-39
7493955-3	1995	We have previously established that PAM and PGL exhibit tandem reaction stereospecificities, with PAM producing, and PGL being reactive toward, only alpha-hydroxyglycine derivatives of absolute configuration (S).	aminohydroxyacetic acid	149-169	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	44-47
7493955-3	1995	We have previously established that PAM and PGL exhibit tandem reaction stereospecificities, with PAM producing, and PGL being reactive toward, only alpha-hydroxyglycine derivatives of absolute configuration (S).	aminohydroxyacetic acid	149-169	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	117-120
8198547-2	1994	Peptidylglycine alpha-amidating mono-oxygenase (PAM; EC 1.14.17.3) catalyses conversion of glycine-extended peptide hormone precursors into their corresponding alpha-hydroxyglycine derivatives.	aminohydroxyacetic acid	160-180	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	0-46
8198547-2	1994	Peptidylglycine alpha-amidating mono-oxygenase (PAM; EC 1.14.17.3) catalyses conversion of glycine-extended peptide hormone precursors into their corresponding alpha-hydroxyglycine derivatives.	aminohydroxyacetic acid	160-180	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	48-51
8198547-10	1994	The stoichiometry between formation of the DMPD cation radical and the alpha-hydroxyglycine PAM product was determined to be 2:1, the value expected for a monooxygenase-catalysed reaction.	aminohydroxyacetic acid	71-91	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	92-95
2059626-4	1991	The monooxygenase first catalyzes formation of the alpha-hydroxyglycine derivative of the glycine-extended precursor, and the lyase subsequently catalyzes breakdown of the PAM product to the amidated peptide and glyoxylate.	aminohydroxyacetic acid	51-71	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	172-175
2265607-7	1990	It was shown that the purified enzyme had converted the model peptide to the C-terminal alpha-hydroxyglycine-extended peptide [X-Gly(OH)] instead of the amidated product (X-NH2), indicating that the enzyme widely known as "PAM" should be called "peptidylglycine alpha-hydroxylating monooxygenase".	aminohydroxyacetic acid	88-108	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	223-226
2265607-7	1990	It was shown that the purified enzyme had converted the model peptide to the C-terminal alpha-hydroxyglycine-extended peptide [X-Gly(OH)] instead of the amidated product (X-NH2), indicating that the enzyme widely known as "PAM" should be called "peptidylglycine alpha-hydroxylating monooxygenase".	aminohydroxyacetic acid	88-108	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	246-296
2207061-0	1990	A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of alpha-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine alpha-amidating monooxygenase in peptide amidation.	aminohydroxyacetic acid	81-101	peptidylglycine alpha-amidating monooxygenase	Bos taurus	153-198
2207061-7	1990	On the basis of these results, we propose that peptide C-terminal amidation in neurointermediate pituitary is a two-step process, with PAM first catalyzing the conversion of a glycine-extended peptide to the alpha-hydroxyglycine derivative, which is in turn converted to the final amide product by HGAD.	aminohydroxyacetic acid	208-228	peptidylglycine alpha-amidating monooxygenase	Bos taurus	135-138
26024288-3	2016	Peptidylamidoglycolate lyase is the PAM domain responsible for the Zn(II)-dependent dealkylation of the alpha-hydroxyglycine-containing precursor to the final alpha-amidated peptide.	aminohydroxyacetic acid	104-124	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	0-28
26024288-3	2016	Peptidylamidoglycolate lyase is the PAM domain responsible for the Zn(II)-dependent dealkylation of the alpha-hydroxyglycine-containing precursor to the final alpha-amidated peptide.	aminohydroxyacetic acid	104-124	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	36-39
19569683-2	2009	Subsequent dealkylation of the alpha-hydroxyglycine by another enzyme, peptidylamidoglycolate lyase (PAL.	aminohydroxyacetic acid	31-51	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	71-99
19170548-0	2009	Involvement of metals in enzymatic and nonenzymatic decomposition of C-terminal alpha-hydroxyglycine to amide: an implication for the catalytic role of enzyme-bound zinc in the peptidylamidoglycolate lyase reaction.	aminohydroxyacetic acid	80-100	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	177-205
10377242-2	1999	C-terminal amidation entails sequential action by peptidylglycine mono-oxygenase (PAM, EC 1.14.17.3) and peptidylamidoglycolate lyase (PGL, EC 4.3.2.5), with the mono-oxygenase catalysing conversion of a glycine-extended pro-peptide into the corresponding alpha-hydroxyglycine derivative, which is then converted by the lyase into amidated peptide plus glyoxylate.	aminohydroxyacetic acid	256-276	peptidylglycine alpha-amidating monooxygenase L homeolog	Xenopus laevis	82-85
9609721-2	1998	The first enzyme activity, peptidylglycine alpha-hydroxylating monooxygenase, catalyzes the oxygen-, ascorbate-, and copper-dependent formation of alpha-hydroxyglycine derivatives.	aminohydroxyacetic acid	147-167	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	27-76