PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8020473-0	1994	A few amino acid substitutions are responsible for the higher thermostability of a novel NAD(+)-dependent bacillar alcohol dehydrogenase.	NAD	89-95	Alcohol dehydrogenase	Escherichia coli	115-136	
8020473-1	1994	The gene adh-hT encoding a thermostable and thermophilic NAD(+)-dependent alcohol dehydrogenase (ADH) from the novel and more thermophilic Bacillus stearothermophilus LLD-R strain was cloned and its nucleotide sequence determined.	NAD	57-63	Alcohol dehydrogenase	Escherichia coli	9-12	
8020473-1	1994	The gene adh-hT encoding a thermostable and thermophilic NAD(+)-dependent alcohol dehydrogenase (ADH) from the novel and more thermophilic Bacillus stearothermophilus LLD-R strain was cloned and its nucleotide sequence determined.	NAD	57-63	Alcohol dehydrogenase	Escherichia coli	74-95	
8020473-1	1994	The gene adh-hT encoding a thermostable and thermophilic NAD(+)-dependent alcohol dehydrogenase (ADH) from the novel and more thermophilic Bacillus stearothermophilus LLD-R strain was cloned and its nucleotide sequence determined.	NAD	57-63	Alcohol dehydrogenase	Escherichia coli	97-100	
23435875-3	2013	In this study, E. coli SZ420 was further engineered for reduction of xylose to xylitol by (1) deleting the alcohol dehydrogenase gene (adhE) to divert NADH from the ethanol pathway; (2) deleting the glucose-specific PTS permease gene (ptsG) to eliminate catabolite repression and allow simultaneous uptake of glucose and xylose; (3) cloning the aldose reductase gene (xylI) of Candida boidinii to reduce xylose to xylitol.	NAD	151-155	Alcohol dehydrogenase	Escherichia coli	107-128	
15549291-6	2005	The resulting two-fold recombinant strain exhibited an in vitro catalytic alcohol dehydrogenase activity of 6.5 units mg-1 protein in reducing methyl acetoacetate to methyl (R)-3-hydroxy butanoate with NADPH as the cofactor and 0.7 units mg-1 protein with NADH.	NAD	256-260	Alcohol dehydrogenase	Escherichia coli	74-95	
15549291-11	2005	Thus, the functional overexpression of alcohol dehydrogenase in the presence of formate dehydrogenase was sufficient to enable and sustain the desired reduction reaction via the relatively low specific activity of alcohol dehydrogenase with NADH, instead of NADPH, as a cofactor.	NAD	241-245	Alcohol dehydrogenase	Escherichia coli	39-60	
15549291-11	2005	Thus, the functional overexpression of alcohol dehydrogenase in the presence of formate dehydrogenase was sufficient to enable and sustain the desired reduction reaction via the relatively low specific activity of alcohol dehydrogenase with NADH, instead of NADPH, as a cofactor.	NAD	241-245	Alcohol dehydrogenase	Escherichia coli	214-235