Substrate specificity of an aflatoxin-metabolizing aldehyde reductase

E M Ellis, J D Hayes

    Research output: Contribution to journalArticlepeer-review

    63 Citations (Scopus)

    Abstract

    The enzyme from rat liver that reduces aflatoxin B1-dialdehyde exhibits a unique catalytic specificity distinct from that of other aldo-keto reductases. This enzyme, designated AFAR, displays high activity towards dicarbonyl-containing compounds with ketone groups on adjacent carbon atoms; 9,10-phenanthrenequinone, acenaphthenequinone and camphorquinone were found to be good substrates. Although AFAR can also reduce aromatic and aliphatic aldehydes such as succinic semialdehyde, it is inactive with glucose, galactose and xylose. The enzyme also exhibits low activity towards alpha,beta-unsaturated carbonyl-containing compounds. Determination of the apparent Km reveals that AFAR has highest affinity for 9,10-phenanthrenequinone and succinic semialdehyde, and low affinity for glyoxal and DL-glyceraldehyde.

    Original languageEnglish
    Pages (from-to)535-41
    Number of pages7
    JournalBiochemical Journal
    Volume312 ( Pt 2)
    DOIs
    Publication statusPublished - 1 Dec 1995

    Keywords

    • Aldehyde Reductase/metabolism
    • Aldehydes/metabolism
    • Animals
    • Carbohydrate Metabolism
    • Cloning, Molecular
    • Enzyme Inhibitors/pharmacology
    • Guinea Pigs
    • Hydrogen-Ion Concentration
    • Kinetics
    • Liver/enzymology
    • Mice
    • Rats
    • Recombinant Proteins/metabolism
    • Structure-Activity Relationship
    • Substrate Specificity

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