Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis

Paul F. Widboom, Elisha N. Fielding, Ye Liu and Steven D. Bruner ()
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Paul F. Widboom: Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, USA
Elisha N. Fielding: Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, USA
Ye Liu: Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, USA
Steven D. Bruner: Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467, USA

Nature, 2007, vol. 447, issue 7142, 342-345

Abstract: Here the authors report the X-ray structure of the vancomycin biosynthetic oxygenation enzyme DpgC — a key enzyme in the biosynthetic pathway of an important class of antibiotics — complexed with a bound substrate mimic. The structure confirms the absence of cofactors in the active site, and electron density consistent with molecular oxygen is present adjacent to the site of oxidation on the substrate, shedding light on the detailed mechanism of cofactor-independent oxygenases.

Date: 2007
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DOI: 10.1038/nature05702

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