PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31703147-5 2019 Next, 3HBOs with a functional carboxyl group (carboxyl form of 3HBO) are obtained by using the alcohol dehydrogenase gene (adhE)-deficient mutant strain, suggesting that the endogenous ethanol produced in E. coli acts as a chain transfer (CT) agent in the generation of 3HBOs. Ethanol 185-192 Alcohol dehydrogenase Escherichia coli 95-116 6986356-1 1980 Mutants of Escherichia coli which overproduce alcohol dehydrogenase were obtained by selection for the ability to use ethanol as an acetate source in a strain auxotrophic for acetate. Ethanol 118-125 Alcohol dehydrogenase Escherichia coli 46-67 6986356-2 1980 A mutant having a 20-fold overproduction of alcohol dehydrogenase was able to use ethanol only to fulfill its acetate requirement, whereas two mutants with a 60-fold overproduction were able to use ethanol as a sole carbon source. Ethanol 82-89 Alcohol dehydrogenase Escherichia coli 44-65 25217026-0 2014 Pyruvate decarboxylase and alcohol dehydrogenase overexpression in Escherichia coli resulted in high ethanol production and rewired metabolic enzyme networks. Ethanol 101-108 Alcohol dehydrogenase Escherichia coli 27-48 29227472-4 2018 Specifically, the enzymes pyruvate decarboxylase and alcohol dehydrogenase have been directed to the filaments, leading to enhanced ethanol production in these engineered bacterial cells compared to those that do not produce the scaffold. Ethanol 132-139 Alcohol dehydrogenase Escherichia coli 53-74 25217026-1 2014 Pyruvate decarboxylase and alcohol dehydrogenase are efficient enzymes for ethanol production in Zymomonas mobilis. Ethanol 75-82 Alcohol dehydrogenase Escherichia coli 27-48 25096392-2 2014 In this study, an ethanologenic Escherichia coli ZY81 was constructed by integrating pyruvate decarboxylase gene pdc and alcohol dehydrogenase gene adhB from Zymomonas mobilis into the genome of E. coli JM109 to obtain the capability of ethanol production. Ethanol 18-25 Alcohol dehydrogenase Escherichia coli 121-142 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. Ethanol 165-172 Alcohol dehydrogenase Escherichia coli 107-128 24020887-7 2013 Deletion of native genes, such as fumarate reductase (frdA) and alcohol dehydrogenase (adhE), responsible for side products succinate and ethanol, which act as electron sink and could compete with butyric acid uptake, did not improve the butanol production efficiency. Ethanol 138-145 Alcohol dehydrogenase Escherichia coli 64-85 24020887-7 2013 Deletion of native genes, such as fumarate reductase (frdA) and alcohol dehydrogenase (adhE), responsible for side products succinate and ethanol, which act as electron sink and could compete with butyric acid uptake, did not improve the butanol production efficiency. Ethanol 138-145 Alcohol dehydrogenase Escherichia coli 87-91 22374228-2 2012 The resulting ethanol pathway involves glycolysis, PDH, and alcohol dehydrogenase (AdhE). Ethanol 14-21 Alcohol dehydrogenase Escherichia coli 60-81 22374228-2 2012 The resulting ethanol pathway involves glycolysis, PDH, and alcohol dehydrogenase (AdhE). Ethanol 14-21 Alcohol dehydrogenase Escherichia coli 83-87 17259366-6 2007 Anaerobic ethanol production by this mutant is apparently the result of a novel pathway that combines the activities of pyruvate dehydrogenase (typically active during aerobic, oxidative metabolism) with the fermentative alcohol dehydrogenase. Ethanol 10-17 Alcohol dehydrogenase Escherichia coli 221-242