High concentrations of aldehydes slow the reaction of cytoplasmic aldehyde dehydrogenase with thiol-group modifiers.
High concentrations of aldehydes slow the inactivation of cytoplasmic aldehyde dehydrogenase by disulfiram and also slow the reaction of the enzyme with 2,2'-dithiodipyridine. It is concluded that a low-affinity aldehyde-binding site is probably the site at which thiol-group modifiers react with aldehyde dehydrogenase, as well as being the active site for hydrolysis of 4-nitrophenyl acetate.
D015082:2,2'-Dipyridyl / Q000031:analogs & derivatives / Q000494:pharmacology*; D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors*; D000447:Aldehydes / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D003593:Cytoplasm / Q000201:enzymology; D004220:Disulfides; D004221:Disulfiram / Q000494:pharmacology*; D011725:Pyridines / Q000494:pharmacology*; D012756:Sheep; D013053:Spectrophotometry
D000447:Aldehydes; D004220:Disulfides; D011725:Pyridines; C001105:2,2'-dipyridyl disulfide; D015082:2,2'-Dipyridyl; D000444:Aldehyde Dehydrogenase; D004221:Disulfiram