PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1301596-6	1992	Recently, powerful irreversible inhibitors of AdoMetDC have become available including 5"-([(Z)-4-amino-2-butenyl]methylamino)-5"-deoxyadenosine, an enzyme activated inhibitor and 5"-deoxy-5"-[(3-hydrazinopropyl)methylamino]adenosine which binds to the active site and forms a covalent bond with the pyruvate prosthetic group.	Pyruvic Acid	300-308	adenosylmethionine decarboxylase 1	Homo sapiens	46-54	
12686127-4	2003	Ornithine decarboxylase is a PLP-requiring decarboxylase, whereas S-adenosylmethionine decarboxylase (AdoMetDC) contains a covalently bound pyruvate prosthetic group.	Pyruvic Acid	140-148	adenosylmethionine decarboxylase 1	Homo sapiens	66-100	
12686127-4	2003	Ornithine decarboxylase is a PLP-requiring decarboxylase, whereas S-adenosylmethionine decarboxylase (AdoMetDC) contains a covalently bound pyruvate prosthetic group.	Pyruvic Acid	140-148	adenosylmethionine decarboxylase 1	Homo sapiens	102-110	
8132508-2	1994	Mammalian S-adenosylmethionine decarboxylase (AdoMetDC) is known to be regulated by putrescine in two ways: (a) acceleration of the rate of conversion of the proenzyme into the mature enzyme in a reaction that forms the pyruvate prosthetic group and (b) activation of the mature enzyme activity.	Pyruvic Acid	220-228	adenosylmethionine decarboxylase 1	Homo sapiens	10-44	
8132508-2	1994	Mammalian S-adenosylmethionine decarboxylase (AdoMetDC) is known to be regulated by putrescine in two ways: (a) acceleration of the rate of conversion of the proenzyme into the mature enzyme in a reaction that forms the pyruvate prosthetic group and (b) activation of the mature enzyme activity.	Pyruvic Acid	220-228	adenosylmethionine decarboxylase 1	Homo sapiens	46-54	
9353291-1	1997	S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl enzyme, and the pyruvate is formed in an intramolecular reaction that cleaves a proenzyme precursor and converts a serine residue into pyruvate.	Pyruvic Acid	76-84	adenosylmethionine decarboxylase 1	Homo sapiens	0-34	
9353291-1	1997	S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl enzyme, and the pyruvate is formed in an intramolecular reaction that cleaves a proenzyme precursor and converts a serine residue into pyruvate.	Pyruvic Acid	76-84	adenosylmethionine decarboxylase 1	Homo sapiens	36-44	
9353291-1	1997	S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl enzyme, and the pyruvate is formed in an intramolecular reaction that cleaves a proenzyme precursor and converts a serine residue into pyruvate.	Pyruvic Acid	195-203	adenosylmethionine decarboxylase 1	Homo sapiens	0-34	
9353291-1	1997	S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl enzyme, and the pyruvate is formed in an intramolecular reaction that cleaves a proenzyme precursor and converts a serine residue into pyruvate.	Pyruvic Acid	195-203	adenosylmethionine decarboxylase 1	Homo sapiens	36-44	
1637820-5	1992	These results indicate that MHZPA inactivates AdoMetDC by forming a hydrazone derivative at the pyruvate prosthetic group.	Pyruvic Acid	96-104	adenosylmethionine decarboxylase 1	Homo sapiens	46-54	
1637820-11	1992	Since the pyruvate is covalently linked to the protein, its replacement by alanine leads to an irreversible inactivation of AdoMetDC.	Pyruvic Acid	10-18	adenosylmethionine decarboxylase 1	Homo sapiens	124-132