Enzyme-catalyzed organic synthesis: NAD(P)H cofactor regeneration using ethanol/alcohol dehydrogenase/aldehyde dehydrogenase and methanol/alcohol dehydrogenase/aldehyde dehydrogenase/formate dehydrogenase

1982 ◽  
Vol 47 (14) ◽  
pp. 2816-2818 ◽  
Author(s):  
Chi Huey Wong ◽  
George M. Whitesides
Keyword(s):  
Alcohol Dehydrogenase ◽  
Organic Synthesis ◽  
Aldehyde Dehydrogenase ◽  
Formate Dehydrogenase ◽  
Cofactor Regeneration

TADH, the thermostable alcohol dehydrogenase from Thermus sp. ATN1: a versatile new biocatalyst for organic synthesis

2008 ◽  
Vol 81 (2) ◽  
pp. 263-273 ◽  
Author(s):  
Volker Höllrigl ◽  
Frank Hollmann ◽  
Andreas C. Kleeb ◽  
Katja Buehler ◽  
Andreas Schmid
Keyword(s):  
Alcohol Dehydrogenase ◽  
Organic Synthesis

Alcohol and aldehyde dehydrogenase activity in the stomach and small intestine of rats poisoned with methanol

2001 ◽  
Vol 20 (5) ◽  
pp. 255-258
Author(s):  
L Chrostek ◽  
D Szczepura ◽  
M Szmitkowski ◽  
W Jelski ◽  
J Wierzchowski
Keyword(s):  
Small Intestine ◽  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Protein Denaturation ◽  
Cell Damage ◽  
Sublethal Dose ◽  
Adh Activity ◽  
Aldehyde Dehydrogenase Activity

The activities of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured with fluorogenic naphthaldehydes in the stomach and small intestine homogenates of rats dosed with 6 g methanol/kg bw after 6, 12, 24 h and 2, 5, 7 days. After intoxication with a sublethal dose, the ADH activity measured with these naphthaldehydes andALDH activities in the stomach and small intestine were significantly decreased. This inhibition is stronger in the stomach and probably depends on cell damage and protein denaturation. We conclude that the activity measured with 6-methoxy-2-naphthaldehyde (MONAL-62) may be due to the activity of rat ADH-1 isoenzyme, and the activity detected with 4-methoxy-1-naphthaldehyde (MONAL-41) to the activity of rat ADH-2 isoenzyme.

Enzymes in organic synthesis. 32. Stereospecific horse liver alcohol dehydrogenase-catalyzed oxidations of exo- and endo-oxabicyclic meso diols

1984 ◽  
Vol 62 (11) ◽  
pp. 2578-2582 ◽  
Author(s):  
J. Bryan Jones ◽  
Christopher J. Francis
Keyword(s):  
Alcohol Dehydrogenase ◽  
Organic Synthesis ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Preparative Scale ◽  
Enantiomerically Pure ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
One Step ◽  
Catalyzed Oxidation ◽  
Enzymes In Organic Synthesis

Preparative-scale horse liver alcohol dehydrogenase-catalyzed oxidation of mesoexo- and endo-7-oxabicyclo[2.2.1]heptane diols provides a direct one-step route to enantiomerically pure chiral γ-lactones of the oxabicyclic series.

Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase Activity in the Serum of Patients with Non-alcoholic Fatty Liver Disease

2018 ◽  
Vol 38 (7) ◽  
pp. 4005-4009 ◽  
Author(s):  
WOJCIECH JELSKI ◽  
BLANKA WOLSZCZAK-BIEDRZYCKA ◽  
ELŻBIETA ZASIMOWICZ-MAJEWSKA ◽  
KAROLINA ORYWAL ◽  
TADEUSZ WOJCIECH LAPINSKI ◽  
...  
Keyword(s):  
Liver Disease ◽  
Alcohol Dehydrogenase ◽  
Fatty Liver ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Fatty Liver Disease ◽  
Alcohol Dehydrogenase Isoenzymes ◽  
Alcoholic Fatty Liver ◽  
Alcoholic Fatty Liver Disease ◽  
Aldehyde Dehydrogenase Activity

Enzyme-coupled measurement of ethanol in whole blood and plasma with a centrifugal analyzer.

1978 ◽  
Vol 24 (6) ◽  
pp. 873-876 ◽  
Author(s):  
G Jung ◽  
G Férard
Keyword(s):  
Alcohol Dehydrogenase ◽  
Aldehyde Dehydrogenase ◽  
Whole Blood ◽  
Detection Limits ◽  
Ethanol Determination

Abstract We describe an automated enzymic method for ethanol determination with a centrifugal analyzer (the GEMSAEC) by measuring the rate of the reaction catalyzed by alcohol dehydrogenase and coupled to aldehyde dehydrogenase. The detection limits, reproducibility, and accuracy of the method have been evaluated. It can be applied to whole blood or plasma, with or without previous deproteinization. Our results, compared with those by an automated alcohol dehydrogenase method in the presence of semicarbazide, show an improved linearity, sensitivity, and rapidity of determination.

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