Inhibition of the dehydrogenase activity of sheep liver cytoplasmic aldehyde dehydrogenase by magnesium ions

Biochemistry ◽  
1983 ◽  
Vol 22 (4) ◽  
pp. 776-784 ◽  
Author(s):  
Adrian F. Bennett ◽  
Paul D. Buckley ◽  
Leonard F. Blackwell
Keyword(s):  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Magnesium Ions ◽  
Sheep Liver

scholarly journals Studies on the interaction between disulfiram and sheep liver cytoplasmic aldehyde dehydrogenase

1978 ◽  
Vol 175 (1) ◽  
pp. 83-90 ◽  
Author(s):  
T M Kitson
Keyword(s):  
Enzyme Activity ◽  
Linear Relationship ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Esterase Activity ◽  
Competitive Inhibitor ◽  
Enzyme Molecule ◽  
Covalent Interaction ◽  
Sheep Liver ◽  
Non Linear

The effect of disulfiram, [1-14C]disulfiram and some other thiol reagents on the activity of cytoplasmic aldehyde dehydrogenase from sheep liver was studied. The results are consistent with a rapid covalent interaction between disulfiram and the enzyme, and inconsistent with the notion that disulfiram is a reversible competitive inhibitor of cytoplasmic aldehyde dehydrogenase. There is a non-linear relationship between loss of about 90% of the enzyme activity and amount of disulfiram added; possible reasons for this are discussed. The remaining approx. 10% of activity is relatively insensitive to disulfiram. It is found that modification of only a small number of groups (one to two) per tetrameric enzyme molecule is responsible for the observed loss of activity. The dehydrogenase activity of the enzyme is affected more severely by disulfiram than is the esterase activity. Negatively charged thiol reagents have little or no effect on cytoplasmic aldehyde dehydrogenase. 2,2′-Dithiodipyridine is an activator of the enzyme.

scholarly journals Effect of some thiocarbamate compounds on aldehyde dehydrogenase and implications for the disulfiram ethanol reaction

1991 ◽  
Vol 278 (1) ◽  
pp. 189-192 ◽  
Author(s):  
T M Kitson
Keyword(s):  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Esterase Activity ◽  
Negligible Effect ◽  
Weak Inhibitor ◽  
Low Concentration ◽  
The Third ◽  
Sheep Liver ◽  
Physiological Phenomenon

The effects of S-methyl diethyldithiocarbamate, S-methyl diethylmonothiocarbamate and bis(diethylcarbamoyl) disulphide on sheep liver cytoplasmic aldehyde dehydrogenase were investigated in vitro. The first compound has negligible effect. The second one is a weak inhibitor of the esterase activity of the enzyme and a weaker inhibitor of the dehydrogenase activity. A very low concentration of the third compound, however, acts as a potent inactivator of aldehyde dehydrogenase, similar in this respect to disulfiram, although somewhat slower to react. The possible involvement of these compounds in the physiological phenomenon known as the disulfiram ethanol reaction is discussed.

Diminished alcohol preference in transgenic mice lacking aldehyde dehydrogenase activity

2002 ◽  
Vol 12 (8) ◽  
pp. 621-626 ◽  
Author(s):  
Toyohi Isse ◽  
Tsunehiro Oyama ◽  
Kyoko Kitagawa ◽  
Koji Matsuno ◽  
Akiko Matsumoto ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Dehydrogenase Activity ◽  
Aldehyde Dehydrogenase ◽  
Alcohol Preference ◽  
Aldehyde Dehydrogenase Activity

scholarly journals Reaction between sheep liver mitochondrial aldehyde dehydrogenase and various thiol-modifying reagents

1989 ◽  
Vol 261 (1) ◽  
pp. 281-284 ◽  
Author(s):  
K M Loomes ◽  
T M Kitson
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Related Compound ◽  
Physiological Responses ◽  
Enzymic Activity ◽  
Cysteine Residues ◽  
Mitochondrial Enzyme ◽  
Step Process ◽  
Cytoplasmic Enzyme ◽  
Sheep Liver

Sheep liver mitochondrial aldehyde dehydrogenase reacts with 2,2′-dithiodipyridine and 4,4′-dithiodipyridine in a two-step process: an initial rapid labelling reaction is followed by slow displacement of the thiopyridone moiety. With the 4,4′-isomer the first step results in an activated form of the enzyme, which then loses activity simultaneously with loss of the label (as has been shown to occur with the cytoplasmic enzyme). With 2,2′-dithiodipyridine, however, neither of the two steps of the reaction has any effect on the enzymic activity, showing that the mitochondrial enzyme possesses two cysteine residues that must be more accessible or reactive (to this reagent at least) than the postulated catalytically essential residue. The symmetrical reagent 5,5′-dithiobis-(1-methyltetrazole) activates mitochondrial aldehyde dehydrogenase approximately 4-fold, whereas the smaller related compound methyl l-methyltetrazol-5-yl disulphide is a potent inactivator. These results support the involvement of mixed methyl disulphides in causing unpleasant physiological responses to ethanol after the ingestion of certain antibiotics.

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.

scholarly journals Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase

1985 ◽  
Vol 225 (1) ◽  
pp. 159-165 ◽  
Author(s):  
F M Dickinson
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Kinetic Studies ◽  
Dissociation Reaction ◽  
Quenching Effect ◽  
Sheep Liver ◽  
Association Reaction ◽  
Hydrolysis Of

The dissociation of the aldehyde dehydrogenase X NADH complex was studied by displacement with NAD+. The association reaction of enzyme and NADH was also studied. These processes are biphasic, as shown by McGibbon, Buckley & Blackwell [(1977) Biochem. J. 165, 455-462], but the details of the dissociation reaction are significantly different from those given by those authors. Spectral and kinetic experiments provide evidence for the formation of abortive complexes of the type enzyme X NADH X aldehyde. Kinetic studies at different wavelengths with transcinnamaldehyde as substrate provide evidence for the formation of an enzyme X NADH X cinnamoyl complex. Hydrolysis of the thioester relieves a severe quenching effect on the fluorescence of enzyme-bound NADH.

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