PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22155126-2	2012	Members of the Acetobacter and Gluconacetobacter genera are capable of transforming EtOH into AcH via the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes and are used for the industrial production of vinegar.	Acetic Acid	222-229	D719_p1008	Acetobacter pasteurianus	138-160	
22155126-2	2012	Members of the Acetobacter and Gluconacetobacter genera are capable of transforming EtOH into AcH via the alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes and are used for the industrial production of vinegar.	Acetic Acid	222-229	D719_p1008	Acetobacter pasteurianus	162-166	
11166817-5	2001	In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7.	Acetic Acid	215-226	D719_p1008	Acetobacter pasteurianus	49-71	
22950009-7	2012	Addition of phenol red to the medium confirmed the ethanol-dependent acidification around the inoculated spots of the clones without transposon insertion, suggesting that casein degradation is due to the production of acetic acid as a result of the combined activities of the alcohol dehydrogenase and ALDH.	Acetic Acid	218-229	D719_p1008	Acetobacter pasteurianus	302-306	
11166817-5	2001	In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7.	Acetic Acid	215-226	D719_p1008	Acetobacter pasteurianus	149-171	
11166817-5	2001	In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7.	Acetic Acid	215-226	D719_p1008	Acetobacter pasteurianus	173-177	
33174682-3	2021	Here, we show that the synergistic regulation of alcohol/aldehyde dehydrogenase expression and cofactor PQQ level could not only efficiently relieve conflict between increased acetic acid production and compromised cell fitness, but also greatly enhance acetic acid tolerance of Acetobacter pasteurianus to a high initial concentration (3% v/v) of acetic acid.	Acetic Acid	176-187	D719_p1008	Acetobacter pasteurianus	57-79	
33174682-3	2021	Here, we show that the synergistic regulation of alcohol/aldehyde dehydrogenase expression and cofactor PQQ level could not only efficiently relieve conflict between increased acetic acid production and compromised cell fitness, but also greatly enhance acetic acid tolerance of Acetobacter pasteurianus to a high initial concentration (3% v/v) of acetic acid.	Acetic Acid	254-265	D719_p1008	Acetobacter pasteurianus	57-79	
33174682-3	2021	Here, we show that the synergistic regulation of alcohol/aldehyde dehydrogenase expression and cofactor PQQ level could not only efficiently relieve conflict between increased acetic acid production and compromised cell fitness, but also greatly enhance acetic acid tolerance of Acetobacter pasteurianus to a high initial concentration (3% v/v) of acetic acid.	Acetic Acid	254-265	D719_p1008	Acetobacter pasteurianus	57-79