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Oxidative stress is a complicating factor in diabetes, inducing non\u2010enzymatic glucose\u2010mediated reactions that change protein structures and impair enzyme functions. We have studied the effects of high glucose, fructose and ribose concentrations on \u03b4\u2010ALA\u2010D activity in vitro. These reducing sugars inhibited \u03b4\u2010ALA\u2010D with efficacies in the order fructose = ribose &gt; glucose. The possible mechanism of glucose inhibition was investigated using lysine, DTT, and <jats:italic>t<\/jats:italic>\u2010butylamine. Oxidation of the enzyme's critical sulfhydryl groups was not involved because DTT had no effect. We concluded that high concentrations of reducing sugars or their autoxidation products inhibit \u03b4\u2010ALA\u2010D by a mechanism not related to thiol oxidation. Also, we are not able to demonstrate that the formation of a Schiff base with the critical lysine residue of the enzyme is involved in the inhibition of \u03b4\u2010ALA\u2010D by hexoses.<\/jats:p>","DOI":"10.1016\/j.cellbi.2005.03.017","type":"journal-article","created":{"date-parts":[[2005,6,24]],"date-time":"2005-06-24T13:42:03Z","timestamp":1119620523000},"page":"669-674","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Human erythrocyte \u03b4\u2010aminolevulinate dehydratase inhibition by monosaccharides is not mediated by oxidation of enzyme sulfhydryl 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