PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29991557-4	2018	Based upon the observation that 1 subunit of succinyl-CoA synthetase (SCS) physically interacts with the first enzyme of heme synthesis (5-aminolevulinate synthase 2, ALAS2) in erythroid cells, it has been posited that succinyl-CoA for ALA synthesis is provided by the adenosine triphosphate-dependent reverse SCS reaction.	succinyl-coenzyme A	45-57	5'-aminolevulinate synthase 2	Homo sapiens	167-172	
32499479-3	2020	Here, we report the human ALAS2 crystal structure, revealing that its Ct-extension folds onto the catalytic core, sits atop the active site, and precludes binding of substrate succinyl-CoA.	succinyl-coenzyme A	176-188	5'-aminolevulinate synthase 2	Homo sapiens	26-31	
30737140-11	2019	Decreased ALAS2 activity results either directly from loss-of-function ALAS2 mutations as seen in X-linked sideroblastic anemia (XLSA) or from defect in the availability of one of its two mitochondrial substrates: glycine in SLC25A38 mutations and succinyl CoA in GLRX5 mutations.	succinyl-coenzyme A	248-260	5'-aminolevulinate synthase 2	Homo sapiens	10-15	
30678654-6	2019	RESULTS: The five ALAS2 single nucleotide variants had from 1.3- to 1.9-fold increases in succinyl-CoA Vmax and 2- to 3-fold increases in thermostability suggesting that most could be gain-of-function modifiers of porphyria instead of causes.	succinyl-coenzyme A	90-102	5'-aminolevulinate synthase 2	Homo sapiens	18-23	
30678654-8	2019	The five novel ALAS2 truncation mutations had increased Vmax values for both succinyl-CoA and glycine substrates (1.4 to 5.6-fold over wild-type), while the Kms for both substrates were only modestly changed.	succinyl-coenzyme A	77-89	5'-aminolevulinate synthase 2	Homo sapiens	15-20	
22740690-6	2012	In contrast, vitamin B6-responsive XLSA mutations p.Arg452Cys and p.Arg452His, with normal in vitro enzyme activity and stability, did not interfere with binding to SUCLA2 but instead had loss of positive cooperativity for succinyl-CoA binding, an increased K(m) for succinyl-CoA, and reduced vitamin B6 affinity.	succinyl-coenzyme A	223-235	5'-aminolevulinate synthase 2	Homo sapiens	35-39	
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.	succinyl-coenzyme A	130-142	5'-aminolevulinate synthase 2	Homo sapiens	28-32	
26300302-8	2015	We propose that (1) the XLPP mutations destabilize the succinyl-CoA-induced hALAS2 closed conformation and thus accelerate ALA release, (2) the extended C-terminus of wild-type mammalian ALAS2 provides a regulatory role that allows for allosteric modulation of activity, thereby controlling the rate of erythroid heme biosynthesis, and (3) this control is disrupted in XLPP, resulting in porphyrin accumulation.	succinyl-coenzyme A	55-67	5'-aminolevulinate synthase 2	Homo sapiens	76-82	
26300302-8	2015	We propose that (1) the XLPP mutations destabilize the succinyl-CoA-induced hALAS2 closed conformation and thus accelerate ALA release, (2) the extended C-terminus of wild-type mammalian ALAS2 provides a regulatory role that allows for allosteric modulation of activity, thereby controlling the rate of erythroid heme biosynthesis, and (3) this control is disrupted in XLPP, resulting in porphyrin accumulation.	succinyl-coenzyme A	55-67	5'-aminolevulinate synthase 2	Homo sapiens	77-82	
25450364-3	2014	ALAS2 is a mitochondrial enzyme, which utilizes glycine and succinyl-CoA to form 5-aminolevulinic acid (ALA), a crucial precursor in heme synthesis.	succinyl-coenzyme A	60-72	5'-aminolevulinate synthase 2	Homo sapiens	0-5	
22740690-6	2012	In contrast, vitamin B6-responsive XLSA mutations p.Arg452Cys and p.Arg452His, with normal in vitro enzyme activity and stability, did not interfere with binding to SUCLA2 but instead had loss of positive cooperativity for succinyl-CoA binding, an increased K(m) for succinyl-CoA, and reduced vitamin B6 affinity.	succinyl-coenzyme A	267-279	5'-aminolevulinate synthase 2	Homo sapiens	35-39	
10727444-7	2000	Because the D190V mutant was identified in a patient with pyridoxine-refractory X-linked sideroblastic anemia, our findings suggest that appropriate association of SCS-betaA and ALAS-E promotes efficient use of succinyl CoA by ALAS-E or helps translocate ALAS-E into mitochondria.	succinyl-coenzyme A	211-223	5'-aminolevulinate synthase 2	Homo sapiens	178-184	
10727444-7	2000	Because the D190V mutant was identified in a patient with pyridoxine-refractory X-linked sideroblastic anemia, our findings suggest that appropriate association of SCS-betaA and ALAS-E promotes efficient use of succinyl CoA by ALAS-E or helps translocate ALAS-E into mitochondria.	succinyl-coenzyme A	211-223	5'-aminolevulinate synthase 2	Homo sapiens	227-233	
10727444-7	2000	Because the D190V mutant was identified in a patient with pyridoxine-refractory X-linked sideroblastic anemia, our findings suggest that appropriate association of SCS-betaA and ALAS-E promotes efficient use of succinyl CoA by ALAS-E or helps translocate ALAS-E into mitochondria.	succinyl-coenzyme A	211-223	5'-aminolevulinate synthase 2	Homo sapiens	227-233	
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.	succinyl-coenzyme A	119-138	5'-aminolevulinate synthase 2	Homo sapiens	23-28