PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12526667-0	2003	Insights into the acylation mechanism of class A beta-lactamases from molecular dynamics simulations of the TEM-1 enzyme complexed with benzylpenicillin.	Penicillin G	136-152	CD248 molecule	Homo sapiens	108-113	
19791786-3	2009	We have investigated the first step in acylation (the formation of the tetrahedral intermediate) for the reaction of benzylpenicillin in the TEM-1 enzyme using high level combined quantum mechanics/molecular mechanics (QM/MM) methods.	Penicillin G	117-133	CD248 molecule	Homo sapiens	141-146	
19538149-3	2009	Thus, penicillin G was undermined by swift accumulation of staphylococcal penicillinase, ampicillin by TEM-1 enzyme and modern oxymino cephalosporins by "extended-spectrum" beta-lactamases.	Penicillin G	6-18	CD248 molecule	Homo sapiens	103-108	
2834979-4	1988	Using TEM-1 as the model beta-lactamase, a Km of 46 microM was observed with benzylpenicillin serving as the substrate.	Penicillin G	77-93	CD248 molecule	Homo sapiens	6-11	
8756327-2	1996	The boronate inhibitor was designed based on the crystallographic coordinates of the acyl-enzyme intermediate of TEM-1 bound to the substrate penicillin G.	Penicillin G	142-154	CD248 molecule	Homo sapiens	113-118