PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3085590-0	1986	Modification of an essential amino group of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal phosphate and by pyridoxal phosphate-sensitized photooxidation.	Pyridoxal Phosphate	97-116	MLO-like protein 4	Zea mays	44-75	
3085590-0	1986	Modification of an essential amino group of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal phosphate and by pyridoxal phosphate-sensitized photooxidation.	Pyridoxal Phosphate	124-143	MLO-like protein 4	Zea mays	44-75	
3085590-1	1986	Phosphoenolpyruvate carboxylase from maize leaves was inactivated by pyridoxal 5"-phosphate in the dark and in the light.	Pyridoxal Phosphate	69-91	MLO-like protein 4	Zea mays	0-31	
3085590-3	1986	Spectral analysis of pyridoxal 5"-phosphate-modified phosphoenolpyruvate carboxylase showed absorption maxima at 432 and 327 nm, before and after reduction with NaBH4, respectively, suggesting that epsilon-amino groups of lysine residues are the reactive groups in the enzyme.	Pyridoxal Phosphate	21-43	MLO-like protein 4	Zea mays	53-84	
9048897-0	1997	Desensitization to glucose 6-phosphate of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal 5"-phosphate.	Pyridoxal Phosphate	95-117	MLO-like protein 4	Zea mays	42-73	
2268676-0	1990	Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5"-phosphate.	Pyridoxal Phosphate	112-134	MLO-like protein 4	Zea mays	65-96	
2268676-1	1990	An active-site peptide from maize (Zea mays L.) phosphoenolpyruvate carboxylase has been isolated, sequenced and identified in the primary structure following chemical modification/inactivation of the enzyme by pyridoxal 5"-phosphate and reduction with sodium borohydride.	Pyridoxal Phosphate	211-233	MLO-like protein 4	Zea mays	48-79