PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35054318-5	2022	The erythroid-specific ALAS2 catalyses the synthesis of delta-aminolevulinic acid (ALA), from the union of glycine and succinyl-coenzyme A, in the first step of the pathway in the erythron.	Aminolevulinic Acid	56-81	5'-aminolevulinate synthase 2	Homo sapiens	23-28	
34492704-10	2021	We further show that itaconyl-CoA is a competitive inhibitor of the erythroid-specific 5-aminolevulinate synthase (ALAS2), the first and rate-limiting step in heme synthesis.	Aminolevulinic Acid	87-104	5'-aminolevulinate synthase 2	Homo sapiens	115-120	
35054318-5	2022	The erythroid-specific ALAS2 catalyses the synthesis of delta-aminolevulinic acid (ALA), from the union of glycine and succinyl-coenzyme A, in the first step of the pathway in the erythron.	Aminolevulinic Acid	83-86	5'-aminolevulinate synthase 2	Homo sapiens	23-28	
35054318-6	2022	In XLP, ALAS2 activity increases, resulting in the amplified formation of ALA, and iron becomes the rate-limiting factor for heme synthesis in the erythroid tissue.	Aminolevulinic Acid	74-77	5'-aminolevulinate synthase 2	Homo sapiens	8-13	
26605136-1	2015	5-Aminolevulinate synthase (ALAS) catalyzes the initial step of mammalian heme biosynthesis, the condensation between glycine and succinyl-CoA to produce CoA, CO2, and 5-aminolevulinate.	Aminolevulinic Acid	168-185	5'-aminolevulinate synthase 2	Homo sapiens	28-32	
21653323-7	2011	The rate of 5-aminolevulinate release from Y586F was significantly increased over that of wild-type ALAS2.	Aminolevulinic Acid	12-29	5'-aminolevulinate synthase 2	Homo sapiens	100-105