PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11599178-3	2001	Class I ACS"s catalyze the synthesis of acetyl-CoA from CO2 + 2e-, CoA, and a methyl group, and contain 5 types of subunits (alpha, beta, gamma, delta, and epsilon).	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	56-59	acyl-CoA synthetase short chain family member 2	Homo sapiens	8-11	
11683635-3	2001	Rapid binding of CO2 and a two-electron reduction activates ACS.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	17-20	acyl-CoA synthetase short chain family member 2	Homo sapiens	60-63	
11599178-5	2001	Class III ACS"s catalyze the same reaction as Class I enzymes, but use pyruvate as a source of CO2 and 2e-, and are composed of 2 autonomous proteins, an alpha 2 beta 2 tetramer and a gamma delta heterodimer.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	95-98	acyl-CoA synthetase short chain family member 2	Homo sapiens	10-13	
22616859-4	2012	In this pathway, CODH converts CO2 into CO and ACS generates acetyl-CoA in a reaction involving Ni CO, methyl-Ni and acetyl-Ni as catalytic intermediates.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	31-34	acyl-CoA synthetase short chain family member 2	Homo sapiens	47-50	
28186407-1	2017	Acetyl-CoA synthase (ACS) is a key enzyme in the Wood-Ljungdahl pathway of anaerobic CO2 fixation, which has long been proposed to operate by a novel mechanism involving a series of protein-bound organometallic (Ni-CO, methyl-Ni, and acetyl-Ni) intermediates.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	85-88	acyl-CoA synthetase short chain family member 2	Homo sapiens	0-19	
28186407-1	2017	Acetyl-CoA synthase (ACS) is a key enzyme in the Wood-Ljungdahl pathway of anaerobic CO2 fixation, which has long been proposed to operate by a novel mechanism involving a series of protein-bound organometallic (Ni-CO, methyl-Ni, and acetyl-Ni) intermediates.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	85-88	acyl-CoA synthetase short chain family member 2	Homo sapiens	21-24	
25416390-4	2014	Use of CO as metabolic fuel for microbes relies on enzymes like carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS), which catalyze conversions resembling processes that eventually initiated the dawn of life.CODHs catalyze the (reversible) oxidation of CO with water to CO2 and come in two different flavors with unprecedented active site architectures.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	285-288	acyl-CoA synthetase short chain family member 2	Homo sapiens	105-124	
25416390-4	2014	Use of CO as metabolic fuel for microbes relies on enzymes like carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS), which catalyze conversions resembling processes that eventually initiated the dawn of life.CODHs catalyze the (reversible) oxidation of CO with water to CO2 and come in two different flavors with unprecedented active site architectures.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	285-288	acyl-CoA synthetase short chain family member 2	Homo sapiens	126-129	
25416390-7	2014	Ni- and Fe-containing CODHs are frequently associated with ACS, where the CODH component reduces CO2 to CO and ACS condenses CO with a methyl group and CoA to acetyl-CoA.Our current state of knowledge on how the three enzymes catalyze these reactions will be summarized and the different strategies of CODHs to achieve the same task within different active site architectures compared.	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	97-100	acyl-CoA synthetase short chain family member 2	Homo sapiens	59-62	
23713976-3	2013	In particular, we unravel the existence of an elusive, dynamically formed gas channel, which CO2 takes to diffuse from the solvent to the active site (C-cluster) of the bifunctional multisubunit enzyme complex carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS).	N2,N6-bis(4-(2-aminoethoxy)quinolin-2-yl)-4-((4-fluorobenzyl)oxy)pyridine-2,6-dicarboxamide	93-96	acyl-CoA synthetase short chain family member 2	Homo sapiens	261-269