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Applied Microbiology and Biotechnology

, Volume 86, Issue 3, pp 791–804 | Cite as

Cofactor-independent oxidases and oxygenases

  • Susanne Fetzner
  • Roberto A. Steiner
Mini-Review

Abstract

Whereas the majority of O2-metabolizing enzymes depend on transition metal ions or organic cofactors for catalysis, a significant number of oxygenases and oxidases neither contain nor require any cofactor. Among the cofactor-independent oxidases, urate oxidase, coproporphyrinogen oxidase, and formylglycine-generating enzyme are of mechanistic as well as medical interest. Formylglycine-generating enzyme is also a promising tool for protein engineering as it can be used to equip proteins with a reactive aldehyde function. PqqC, an oxidase in the biosynthesis of the bacterial cofactor pyrroloquinoline quinone, catalyzes an eight-electron ring-closure oxidation reaction. Among bacterial oxygenases, quinone-forming monooxygenases involved in the tailoring of polyketides, the dioxygenase DpgC found in the biosynthesis of a building block of vancomycin and teicoplanin antibiotics, luciferase monooxygenase from Renilla sp., and bacterial ring-cleaving 2,4-dioxygenases active towards 3-hydroxy-4(1H)-quinolones have been identified as cofactor-independent enzymes. Interestingly, the 3-hydroxy-4(1H)-quinolone 2,4-dioxygenases as well as Renilla luciferase use an α/β-hydrolase architecture for oxygenation reactions. Cofactor-independent oxygenases and oxidases catalyze very different reactions and belong to several different protein families, reflecting their diverse origin. Nevertheless, they all may share the common mechanistic concept of initial base-catalyzed activation of their organic substrate and “substrate-assisted catalysis.”

Keywords

Oxygen Oxygenase Oxidase Cofactor-independent enzymes α/β-hydrolase fold 

Notes

Acknowledgments

Work in the laboratory of S.F. on cofactor-independent dioxygenases and on bacterial alkylquinolone metabolism has been supported by grants from the German Research Foundation (Deutsche Forschungsgemeinschaft; FE 383/15-1 and 16-1), which are gratefully acknowledged. This work was also supported by a King’s College London incentive grant to R.A.S.

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© Springer-Verlag 2010

Authors and Affiliations

  1. 1.Institut für Molekulare Mikrobiologie und BiotechnologieWestfälische Wilhelms-Universität MünsterMünsterGermany
  2. 2.Randall Division of Cell and Molecular BiophysicsKing’s College LondonLondonUK

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