PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16459339-3	2006	The crystal structure and the reaction mechanism of SAT from E.coli have shown that the substrate L-serine and the inhibitor L-cysteine bind to the identical region in the SAT protein.	Serine	98-106	streptothricin acetyltransferase	Escherichia coli	52-55	
22179612-2	2012	The complex is comprised of the two enzymes that catalyze the final steps in cysteine biosynthesis: serine O-acetyltransferase (SAT, EC 2.3.1.30), which produces O-acetyl-L-serine, and O-acetyl-L-serine sulfhydrylase (OASS, EC 2.5.1.47), which converts it to cysteine.	Serine	172-179	streptothricin acetyltransferase	Escherichia coli	100-126	
16459339-3	2006	The crystal structure and the reaction mechanism of SAT from E.coli have shown that the substrate L-serine and the inhibitor L-cysteine bind to the identical region in the SAT protein.	Serine	98-106	streptothricin acetyltransferase	Escherichia coli	172-175	
16459339-4	2006	To decrease the affinity for only L-cysteine, we first built the structure model of L-serine-binding SAT on the basis of the crystal structure with bound L-cysteine and compared these two structures.	Serine	84-92	streptothricin acetyltransferase	Escherichia coli	101-104	
12940772-5	2003	Since earlier kinetic studies with SAT from S. typhimurium suggested that cysteine competes with acetyl-CoA for binding, rather than serine with which it is isostructural, the specificity of the serine-binding pocket was assessed with three substrate mimics; beta-hydroxypropionic acid, glycine and ethanolamine.	Serine	195-201	streptothricin acetyltransferase	Escherichia coli	35-38	
15231846-7	2004	On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT.	Serine	123-129	streptothricin acetyltransferase	Escherichia coli	133-136	
12940772-6	2003	The data show that SAT interacts productively with the amino and hydroxymethyl moieties of serine, whereas the carboxyl group provides an essential contribution to binding strongly, supporting a view that cysteine will interact productively at the serine-binding site.	Serine	91-97	streptothricin acetyltransferase	Escherichia coli	19-22	
12940772-8	2003	Such a proposal is supported by the results of micro-calorimetric studies which show that cysteine competes with serine for binding to SAT rather than with CoA.	Serine	113-119	streptothricin acetyltransferase	Escherichia coli	135-138	
12940772-9	2003	It follows that tight binding of cysteine at the serine-binding site near the catalytic centre may be the effector of a substantial reduction in the affinity of SAT for CoA, yielding the observed pattern of steady-state inhibition and the mechanism by which cysteine mediates effective end-product control of its synthesis.	Serine	49-55	streptothricin acetyltransferase	Escherichia coli	161-164	
10542289-7	1999	Biochemical characterization of the recombinant E. histolytica SAT revealed several enzymatic features that distinguished the amoebic enzyme from the bacterial and plant enzymes: 1) inhibition by L-cysteine in a competitive manner with L-serine; 2) inhibition by L-cystine; and 3) no association with cysteine synthase.	Serine	236-244	streptothricin acetyltransferase	Escherichia coli	63-66	
12627979-6	2003	Kinetic data for the reverse reaction (acetylation of CoA by O-acetylserine) are also consistent with a steady-state random-order mechanism, wherein both the breakdown of the SAT*serine complex and the interconversion of ternary complexes are partially rate-determining.	Serine	69-75	streptothricin acetyltransferase	Escherichia coli	175-178	
10052138-3	1999	Analyses of the N- and C-terminal amino acid sequences found that the truncated SAT designated as SAT delta C20 was a resultant form of the wild-type SAT cleaved between Ser 253 and Met 254, deleting 20 amino acid residues from the C-terminus.	Serine	170-173	streptothricin acetyltransferase	Escherichia coli	80-83	
10052138-3	1999	Analyses of the N- and C-terminal amino acid sequences found that the truncated SAT designated as SAT delta C20 was a resultant form of the wild-type SAT cleaved between Ser 253 and Met 254, deleting 20 amino acid residues from the C-terminus.	Serine	170-173	streptothricin acetyltransferase	Escherichia coli	98-101	
10052138-3	1999	Analyses of the N- and C-terminal amino acid sequences found that the truncated SAT designated as SAT delta C20 was a resultant form of the wild-type SAT cleaved between Ser 253 and Met 254, deleting 20 amino acid residues from the C-terminus.	Serine	170-173	streptothricin acetyltransferase	Escherichia coli	98-101