PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1989509-5	1991	Purified SSAT had a specific activity of 285 mumol/min/mg for spermidine and Km values of 5.9 microM for acetylcoenzyme A, 55 microM for spermidine, 5 microM for spermine, 36 microM for N1-acetylspermine, 1.6 microM for norspermidine, and 4 microM for norspermine.	Acetyl Coenzyme A	105-121	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	9-13	
15096507-12	2004	Metabolic effects that were not excluded as possible contributing factors include high levels of putrescine and acetylated polyamines, a 50% reduction in S-adenosylmethionine, and a 45% decline in the SSAT cofactor acetyl-CoA.	Acetyl Coenzyme A	215-225	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	201-205	
19589128-6	2009	SSAT may also influence cellular metabolism via interaction with other proteins and by perturbing the content of acetyl-CoA and ATP.	Acetyl Coenzyme A	113-123	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	0-4	
18690703-1	2008	The enzyme spermidine/spermine N (1)-acetyltransferase (SSAT) catalyzes the transfer of acetyl groups from acetylcoenzyme A to spermidine and spermine, as part of a polyamine degradation pathway.	Acetyl Coenzyme A	107-123	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	56-60	
18349109-10	2008	Transgenic manipulation of SSAT activity has revealed that SSAT activity links polyamine metabolism to lipid and carbohydrate metabolism by means of alterations in the content of acetyl-CoA and ATP.	Acetyl Coenzyme A	179-189	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	27-31	
18349109-10	2008	Transgenic manipulation of SSAT activity has revealed that SSAT activity links polyamine metabolism to lipid and carbohydrate metabolism by means of alterations in the content of acetyl-CoA and ATP.	Acetyl Coenzyme A	179-189	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	59-63	
16455797-3	2006	We have expressed human SSAT from the cloned cDNA in Escherichia coli and have determined high-resolution structures of wild-type and mutant SSAT, as the free dimer and in binary and ternary complexes with CoA, acetyl-CoA (AcCoA), spermine, and the inhibitor N1,N11bis-(ethyl)-norspermine (BE-3-3-3).	Acetyl Coenzyme A	211-221	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	24-28	
16455797-3	2006	We have expressed human SSAT from the cloned cDNA in Escherichia coli and have determined high-resolution structures of wild-type and mutant SSAT, as the free dimer and in binary and ternary complexes with CoA, acetyl-CoA (AcCoA), spermine, and the inhibitor N1,N11bis-(ethyl)-norspermine (BE-3-3-3).	Acetyl Coenzyme A	223-228	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	24-28	
2241897-3	1990	Although other acetylases are capable of acetylating polyamines using acetyl-CoA as the acetyl donor, the greater than 600-fold induction within 24 h was found to be specifically SSAT, since essentially all activity was precipitable by the specific antisera.	Acetyl Coenzyme A	70-80	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	179-183