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Biochemical and structural explorations of α‐hydroxyacid oxidases reveal a four‐electron oxidative decarboxylation reaction

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  • معلومة اضافية
    • بيانات النشر:
      eScholarship, University of California, 2019.
    • الموضوع:
      2019
    • نبذة مختصرة :
      p-Hydroxymandelate oxidase (Hmo) is a flavin mononucleotide (FMN)-dependent enzyme that oxidizes mandelate to benzoylformate. How the FMN-dependent oxidation is executed by Hmo remains unclear at the molecular level. A continuum of snapshots from crystal structures of Hmo and its mutants in complex with physiological/nonphysiological substrates, products and inhibitors provides a rationale for its substrate enantioselectivity/promiscuity, its active-site geometry/reactivity and its direct hydride-transfer mechanism. A single mutant, Y128F, that extends the two-electron oxidation reaction to a four-electron oxidative decarboxylation reaction was unexpectedly observed. Biochemical and structural approaches, including biochemistry, kinetics, stable isotope labeling and X-ray crystallography, were exploited to reach these conclusions and provide additional insights.
    • File Description:
      application/pdf
    • Rights:
      public
    • الرقم المعرف:
      edssch.oai:escholarship.org:ark:/13030/qt0ts55916