PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
11080311-5	2000	The basic biochemical properties of the monofunctional SDH, including its pH optimum as well as the apparent Michaelis constant (K(m)) values for its substrates saccharopine and nicotinamide adenine dinucleotide at neutral and basic pH values, were similar to those of its SDH counterpart that is linked to LKR.	saccharopine	161-173	lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzyme	Arabidopsis thaliana	55-58
17854830-3	2007	A model of the ternary complex of SDH, NAD, and saccharopine identifies residues Lys77 and Glu122 as potentially important for substrate binding and/or catalysis, consistent with a proton shuttle mechanism.	saccharopine	48-60	succinate dehydrogenase complex iron sulfur subunit B	Homo sapiens	34-37
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.	saccharopine	154-166	aminoadipate-semialdehyde synthase	Homo sapiens	14-47
10929113-1	2000	Both plants and animals catabolize lysine via saccharopine by two consecutive enzymes, lysine-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single polypeptide.	saccharopine	46-58	lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzyme	Arabidopsis thaliana	87-117
10929113-1	2000	Both plants and animals catabolize lysine via saccharopine by two consecutive enzymes, lysine-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single polypeptide.	saccharopine	46-58	lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzyme	Arabidopsis thaliana	119-122
10929113-1	2000	Both plants and animals catabolize lysine via saccharopine by two consecutive enzymes, lysine-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single polypeptide.	saccharopine	46-58	Saccharopine dehydrogenase	Arabidopsis thaliana	128-154
10929113-1	2000	Both plants and animals catabolize lysine via saccharopine by two consecutive enzymes, lysine-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single polypeptide.	saccharopine	46-58	Saccharopine dehydrogenase	Arabidopsis thaliana	156-159
12226216-1	1996	The first enzyme of the lysine degradation pathway in maize (Zea mays L.), lysine-ketoglutarate reductase, condenses lysine and [alpha]-ketoglutarate into saccharopine using NADPH as a cofactor, whereas the second, saccharopine dehydrogenase, converts saccharopine to [alpha]-aminoadipic-[delta]-semialdehyde and glutamic acid using NAD+ or NADP+ as a cofactor.	saccharopine	155-167	Probable mitochondrial saccharopine dehydrogenase-like oxidoreductase At5g39410	Zea mays	215-241
35135854-0	2022	The metabolite saccharopine impairs neuronal development by inhibiting the neurotrophic function of glucose-6-phosphate isomerase.	saccharopine	15-27	glucose-6-phosphate isomerase 1	Mus musculus	100-129
35135854-3	2022	Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development.	saccharopine	344-356	aminoadipate-semialdehyde synthase	Mus musculus	20-24
35135854-3	2022	Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development.	saccharopine	344-356	aminoadipate-semialdehyde synthase	Mus musculus	114-117
35135854-3	2022	Here we report that Aass mutant male and female mice carrying the R65Q mutation in alpha-ketoglutarate reductase (LKR) domain have an elevated cerebral lysine level and a normal brain development, whereas the Aass mutant mice carrying the G489E mutation in saccharopine dehydrogenase (SDH) domain exhibit elevations of both cerebral lysine and saccharopine levels and a smaller brain with defective neuronal development.	saccharopine	344-356	aminoadipate-semialdehyde synthase	Mus musculus	209-213
35135854-4	2022	Mechanistically, the accumulated saccharopine, but not lysine, leads to impaired neuronal development by inhibiting the neurotrophic effect of glucose-6-phosphate isomerase (GPI).	saccharopine	33-45	glucose-6-phosphate isomerase 1	Mus musculus	143-172
35135854-4	2022	Mechanistically, the accumulated saccharopine, but not lysine, leads to impaired neuronal development by inhibiting the neurotrophic effect of glucose-6-phosphate isomerase (GPI).	saccharopine	33-45	glucose-6-phosphate isomerase 1	Mus musculus	174-177
35135854-7	2022	Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development.	saccharopine	260-272	aminoadipate-semialdehyde synthase	Mus musculus	70-74
35135854-7	2022	Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development.	saccharopine	260-272	aminoadipate-semialdehyde synthase	Mus musculus	192-195
35135854-7	2022	Here, we report that mice carrying the R65Q mutation in LKR domain of AASS have an elevated cerebral lysine levels and a normal brain development, whereas those carrying the G489E mutation in SDH domain of AASS exhibit an elevation of both cerebral lysine and saccharopine and a small brain with defective neuronal development.	saccharopine	260-272	aminoadipate-semialdehyde synthase	Mus musculus	206-210
35135854-8	2022	Furthermore, saccharopine impairs neuronal development by inhibiting the neurotrophic effect of glucose-6-phosphate isomerase.	saccharopine	13-25	glucose-6-phosphate isomerase 1	Mus musculus	96-125
10859195-1	2000	Both in mammals and plants, excess lysine (Lys) is catabolized via saccharopine into alpha-amino adipic semialdehyde and glutamate by two consecutive enzymes, Lys-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single bifunctional polypeptide.	saccharopine	67-79	lysine-ketoglutarate reductase/saccharopine dehydrogenase bifunctional enzyme	Arabidopsis thaliana	188-191
226150-3	1979	The NMR analysis of the saccharopine prepared with [4"A-2H]NADH revealed that the label was incorporated into the C-2 of the glutaryl moiety.	saccharopine	24-36	complement C2	Homo sapiens	114-117
32567100-6	2020	These in vivo data demonstrate that the saccharopine pathway is the main source of glutaric acid production in the brain and periphery of a mouse model for GA1, and support the notion that pharmacological inhibition of AASS may represent an attractive strategy to treat GA1.	saccharopine	40-52	aminoadipate-semialdehyde synthase	Mus musculus	219-223
30573525-3	2019	In Caenorhbditis elegans, mutations in the saccharopine dehydrogenase (SDH) domain of the bi-functional enzyme alpha-aminoadipic semialdehyde synthase AASS-1 greatly elevate the lysine catabolic intermediate saccharopine, which causes mitochondrial damage by disrupting mitochondrial dynamics, leading to reduced adult animal growth.	saccharopine	43-55	aminoadipate-semialdehyde synthase	Mus musculus	71-74
30573525-5	2019	Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis.	saccharopine	72-84	aminoadipate-semialdehyde synthase	Mus musculus	147-150
30573525-5	2019	Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis.	saccharopine	168-180	aminoadipate-semialdehyde synthase	Mus musculus	147-150
30573525-5	2019	Importantly, genetic inactivation of genes that raise the mitochondrial saccharopine precursors lysine and alpha-ketoglutarate strongly suppresses SDH mutation-induced saccharopine accumulation and mitochondrial abnormalities in C. elegans Thus, adequate saccharopine catabolism is essential for mitochondrial homeostasis.	saccharopine	168-180	aminoadipate-semialdehyde synthase	Mus musculus	147-150
28928432-6	2017	Single mutants in MDH3 or GPD1 grow on lysine-deficient medium, but an mdh3/gpd1Delta double mutant accumulates saccharopine and displays lysine bradytrophy.	saccharopine	112-124	malate dehydrogenase MDH3	Saccharomyces cerevisiae S288C	71-75
27615426-6	2017	Analysis of epsilon-15N and alpha-15N lysine catabolites in plasma, liver and brain suggested the saccharopine as the main pathway for AAA biosynthesis.	saccharopine	98-110	achalasia, adrenocortical insufficiency, alacrimia	Mus musculus	135-138
22449979-0	2012	Lysine degradation through the saccharopine pathway in bacteria: LKR and SDH in bacteria and its relationship to the plant and animal enzymes.	saccharopine	31-43	succinate dehydrogenase complex iron sulfur subunit B	Homo sapiens	73-76
23732302-5	2013	From the point of view of energy, the SDH catalytic reaction for the synthesis of l-lysine is unfavorable compared with its reverse reaction for the synthesis of saccharopine.	saccharopine	162-174	succinate dehydrogenase complex iron sulfur subunit B	Homo sapiens	38-41