Structure of OxyAtei: Completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascadeHaslinger, K. & Cryle, M. J., Feb-2016, In : FEBS Letters. 590, 4, p. 571-81 11 p.
Research output: Contribution to journal › Article › Academic › peer-review
Cyclization of glycopeptide antibiotic precursors occurs in either three or four steps catalyzed by Cytochrome P450 enzymes. Three of these enzymes have been structurally characterized to date with the second enzyme along the pathway, OxyA, escaping structural analysis. We are now able to present the structure of OxyAtei involved in teicoplanin biosynthesis - the same enzyme recently shown to be the first active OxyA homolog. In spite of the hydrophobic character of the teicoplanin precursor, the polar active site of OxyAtei and its affinity for certain azole inhibitors hint at its preference for substrates with polar decorations.
|Number of pages||11|
|Publication status||Published - Feb-2016|
- Amino Acid Sequence, Anti-Bacterial Agents/biosynthesis, Bacterial Proteins/chemistry, Catalytic Domain, Crystallography, X-Ray, Cyclization, Cytochrome P-450 Enzyme System/chemistry, Micromonosporaceae/enzymology, Molecular Sequence Data, Protein Structure, Secondary, Teicoplanin/biosynthesis