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Structural effects on Arthrobacter methylene hydroxylase activity.

S Hayasaka, D A Klein

    Journal of Bacteriology
    |December 1, 1971
    PubMed
    Summary
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    Arthrobacter 4-44-2 can oxidize n-alkanes using methylene hydroxylase. This enzyme

    Area of Science:

    • Microbiology
    • Biochemistry
    • Enzymology

    Background:

    • Arthrobacter 4-44-2 exhibits subterminal oxidation of n-hexadecane.
    • The bacterium produces 2-, 3-, and 4-alcoholic and ketonic products.
    • Understanding the methylene hydroxylase is key to microbial oxidation pathways.

    Purpose of the Study:

    • To investigate the induction and repression of methylene hydroxylase activity in Arthrobacter 4-44-2.
    • To explore structural relationships influencing methylene function oxidation.
    • To identify optimal conditions for enzyme induction and activity.

    Main Methods:

    • Induction of methylene hydroxylase using various n-alkanes and cyclic compounds.
    • Testing substrate specificity with different chain lengths and functional groups.

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  • Utilizing cell-free systems to confirm inducibility.
  • Assessing the effect of acetate on enzyme induction.

    • Main Results:

    • Induction was optimal with n-alkanes (C10-C16) and methylcyclohexane.
    • n-Alkanes (C14-C16) were oxidized to internal products; shorter even-carbon alkanes showed no activity.
    • Hexadecene-1 and alcohols yielded ketonic/aldehydic products.
    • Acetate strongly repressed enzyme induction.
    • Cell-free systems confirmed inducibility, with stimulation by reduced pyridine nucleotides and ferrous ion.

    Conclusions:

    • Methylene hydroxylase activity is inducible by specific n-alkanes and methylcyclohexane.
    • Substrate structure, particularly the methyl group's role in orientation, influences hydroxylation.
    • Acetate acts as a repressor for enzyme induction.
    • The enzyme's activity can be modulated by cofactors in cell-free systems.