PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11286508-1	2001	In mammals, L-lysine is first catabolized to alpha-aminoadipate semialdehyde by the bifunctional enzyme alpha-aminoadipate semialdehyde synthase (AASS), followed by a conversion to alpha-aminoadipate by alpha-aminoadipate semialdehyde dehydrogenase.	Lysine	12-20	aminoadipate-semialdehyde synthase	Homo sapiens	104-144	
16525756-3	2006	The first two enzymes of lysine catabolism are synthesized from a single LKR/SDH gene.	Lysine	25-31	aminoadipate-semialdehyde synthase	Homo sapiens	73-80	
23890588-12	2013	Mutational screening of the AASS gene revealed that case 1 was a compound heterozygote for c.2662 + 1_2662 + 5delGTAAGinsTT and c.874A>G and that case 2 was a compound heterozygote for c.976_977delCA and c.1925C>G. In conclusion, we present two children with hyperlysinemia type I and neurological impairment in which implementation of lysine-restricted diet achieved a mild improvement of symptoms but did not reverse cognitive impairment.	Lysine	270-276	aminoadipate-semialdehyde synthase	Homo sapiens	28-32	
19774086-1	2009	BACKGROUND: Lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) is a bifunctional enzyme catalyzing the first two steps of lysine catabolism in plants and mammals.	Lysine	139-145	aminoadipate-semialdehyde synthase	Homo sapiens	12-69	
19774086-1	2009	BACKGROUND: Lysine-ketoglutarate reductase/saccharopine dehydrogenase (LKR/SDH) is a bifunctional enzyme catalyzing the first two steps of lysine catabolism in plants and mammals.	Lysine	139-145	aminoadipate-semialdehyde synthase	Homo sapiens	71-78	
19774086-2	2009	However, to date, the properties of the lysine degradation pathway and biological functions of LKR/SDH have been very little described in arthropods such as ticks.	Lysine	40-46	aminoadipate-semialdehyde synthase	Homo sapiens	95-102	
10775527-11	2000	On the basis of these and other results, we propose that AASS catalyzes the first two steps of the major lysine-degradation pathway in human cells and that inactivating mutations in the AASS gene are a cause of hyperlysinemia.	Lysine	105-111	aminoadipate-semialdehyde synthase	Homo sapiens	57-61	
10775527-11	2000	On the basis of these and other results, we propose that AASS catalyzes the first two steps of the major lysine-degradation pathway in human cells and that inactivating mutations in the AASS gene are a cause of hyperlysinemia.	Lysine	105-111	aminoadipate-semialdehyde synthase	Homo sapiens	186-190	
4774398-1	1973	The enzymes involved in the initial degradative steps of lysine metabolism, lysine-2-oxoglutarate reductase and saccharopine dehydrogenase, were studied and their activities in different mammals compared.	Lysine	57-63	aminoadipate-semialdehyde synthase	Homo sapiens	76-107	
3110158-0	1987	The bifunctional aminoadipic semialdehyde synthase in lysine degradation.	Lysine	54-60	aminoadipate-semialdehyde synthase	Homo sapiens	17-50	
3110158-2	1987	The mammalian aminoadipic semialdehyde synthase is a bifunctional enzyme that catalyzes the first two sequential steps in lysine degradation in the major saccharopine pathway (Markovitz, P. J., Chuang, D. T., and Cox, R. P. (1984) J. Biol.	Lysine	122-128	aminoadipate-semialdehyde synthase	Homo sapiens	14-47