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Showing 1 to 7 of 7 for “"N-hydroxylating"”.

  1. Mechanistic Studies and Inhibition of N-hydroxylating Monooxygenases

    N-hydroxylating monooxygenases (NMO) are members the class B flavoprotein monooxygenases. They catalyze the N-hydroxylation of lysine and ornithine and play and essential role in the biosynthesis of hydroxamate containing siderophores. Siderophores are high affinity iron-chelators composed of …

    vt Repository record for Mechanistic Studies and Inhibition of N-hydroxylating Monooxygenases (opens in a new tab)

  2. Biochemical characterization of Aspergillus fumigatus SidA: a flavin-dependent N-hydroxylating enzyme

    Ferrichrome is a hydroxamate-containing siderophore produced by the pathogenic fungus Aspergillus fumigatus during infection. This siderophore includes N5-hydroxylated L-ornithine in the peptide backbone that serve as iron chelators. Af SidA is the L-ornithine N5-hydroxylase, which performs the …

    vt Repository record for Biochemical characterization of Aspergillus fumigatus SidA: a flavin-dependent N-hydroxylating enzyme (opens in a new tab)

  3. Structural and Mechanistic Studies on N-Hydroxylating Monooxygenases Involved in Siderophore Biosynthesis

    N-Hydroxylating monooxygenases (NMOs) are flavin dependent enzymes that primarily catalyze the hydroxylation of L-ornithine or L-lysine. This is the first, committed step to siderophore biosynthesis. Pathogenic microbes including Aspergillus fumigatus and Mycobacterium tuberculosis secrete these …

    vt Repository record for Structural and Mechanistic Studies on N-Hydroxylating Monooxygenases Involved in Siderophore Biosynthesis (opens in a new tab)

  4. Biochemical Characterization of Thermocrispum agreste TheA: A Flavin-Dependent N-hydroxylating Enzyme

    N-hydroxylating monooxygenases (NMOs) are Class B flavin-dependent monooxygenases found only in fungi and bacteria. These enzymes catalyze the hydroxylation of nucleophilic primary amines, such as those found in histamine, L-ornithine, L-lysine, and small aliphatic diamines. The hydroxamate moiety …

    vt Repository record for Biochemical Characterization of Thermocrispum agreste TheA: A Flavin-Dependent N-hydroxylating Enzyme (opens in a new tab)

  5. Structural and Mutational Analyses of Aspergillus fumigatus SidA: A Flavin-Dependent N-hydroxylating Enzyme

    SidA from Aspergillus fumigatus is an N-hydroxylating monooxygenase that catalyzes the committed step in siderophore biosynthesis. This gene is essential for virulence making it an excellent drug target. In order to design an inhibitor against SidA a greater understanding of the mechanism and …

    vt Repository record for Structural and Mutational Analyses of Aspergillus fumigatus SidA: A Flavin-Dependent N-hydroxylating Enzyme (opens in a new tab)

  6. Flavin-dependent Enzymes in Natural Product Biosynthesis

    … from Allium sativum (AsFMO) and N-hydroxylating monooxygenase from Streptomyces sp. XY332 (FzmM) were studied. Both enzymes perform heteroatom oxidation as part of allicin or fosfazinomycin biosynthesis respectively. AsFMO was predicted to oxidize S-allyl-L-cysteine (SAC) to alliin …

    vt Repository record for Flavin-dependent Enzymes in Natural Product Biosynthesis (opens in a new tab)

  7. Mechanistic Studies of Flavin-Dependent Monooxygenases Involved in Bacterial Defense and Plant Metabolism

    Flavin-dependent monooxygenases (FMOs) are a large family of enzymes found in microbes, plants, animals, and humans involved in defense pathways, xenobiotic metabolism, and natural product biosynthesis. One class of FMOs, Class B, carries out the oxidation of heteroatomic substrates, via …

    vt Repository record for Mechanistic Studies of Flavin-Dependent Monooxygenases Involved in Bacterial Defense and Plant Metabolism (opens in a new tab)