PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28667034-4	2017	We assume that this amino acid substitution affects the enzymatic activity of ALAS2 by affecting its interaction with the cofactor pyridoxal 5"-phosphate, since the patient was responsive to pyridoxine treatment.	Pyridoxal Phosphate	131-153	5'-aminolevulinate synthase 2	Homo sapiens	78-83	
27838491-1	2017	Mutations in the C-terminus of human erythroid 5-aminolevulinate synthase (hALAS2), a pyridoxal 5"-phosphate (PLP)-dependent enzyme, are associated with two different blood disorders, X-linked sideroblastic anemia (XLSA) and X-linked protoporphyria (XLPP).	Pyridoxal Phosphate	86-108	5'-aminolevulinate synthase 2	Homo sapiens	75-81	
25705881-5	2015	We determined that this mutation (Y365C) impairs binding of the essential cofactor pyridoxal 5"-phosphate to ALAS2, resulting in destabilization of the enzyme and consequent loss of function.	Pyridoxal Phosphate	83-105	5'-aminolevulinate synthase 2	Homo sapiens	109-114