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Structure of OxyA tei : completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade
Author(s) -
Haslinger Kristina,
Cryle Max J.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12081
Subject(s) - glycopeptide , enzyme , teicoplanin , cytochrome p450 , chemistry , stereochemistry , active site , cytochrome , biochemistry , antibiotics , biology , bacteria , vancomycin , genetics , staphylococcus aureus
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 OxyA tei 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 OxyA tei and its affinity for certain azole inhibitors hint at its preference for substrates with polar decorations.