{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,6]],"date-time":"2026-09-06T11:03:02Z","timestamp":1788692582791,"version":"build-2803163510"},"reference-count":77,"publisher":"Wiley","issue":"18","license":[{"start":{"date-parts":[[2014,10,30]],"date-time":"2014-10-30T00:00:00Z","timestamp":1414627200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemBioChem"],"published-print":{"date-parts":[[2014,12,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Bacterial cytochrome P450s form a remarkable clade of the P450 superfamily of oxidative hemoproteins, and are often involved in the biosynthesis of complex natural products. Those in a subgroup known as \u201cOxy enzymes\u201d play a crucial role in the biosynthesis of glycopeptide antibiotics, including vancomycin and teicoplanin. The Oxy enzymes catalyze crosslinking of aromatic residues in the non\u2010ribosomal antibiotic precursor peptide while it remains bound to the non\u2010ribosomal peptide synthetase (NRPS); this crosslinking secures the three\u2010dimensional structure of the glycopeptide, crucial for antibiotic activity. We have characterized OxyB\n                    <jats:sub>tei<\/jats:sub>\n                    , the first of the Oxy enzymes in teicoplanin biosynthesis. Our results reveal that OxyB\n                    <jats:sub>tei<\/jats:sub>\n                    possesses a structure similar to those of other Oxy proteins and is active in crosslinking NRPS\u2010bound peptide substrates. However, OxyB\n                    <jats:sub>tei<\/jats:sub>\n                    displays a significantly altered activity spectrum against peptide substrates compared to its well\u2010studied vancomycin homologue.\n                  <\/jats:p>","DOI":"10.1002\/cbic.201402441","type":"journal-article","created":{"date-parts":[[2014,10,30]],"date-time":"2014-10-30T16:03:17Z","timestamp":1414684997000},"page":"2719-2728","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":55,"title":["Cytochrome P450 OxyB\n                    <sub>tei<\/sub>\n                    Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis"],"prefix":"10.1002","volume":"15","author":[{"given":"Kristina","family":"Haslinger","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Egle","family":"Maximowitsch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clara","family":"Brieke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexa","family":"Koch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Max J.","family":"Cryle","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2014,10,30]]},"reference":[{"key":"e_1_2_6_1_2","unstructured":"\u00a0"},{"key":"e_1_2_6_2_2","first-page":"1","volume-title":"Amino Acids, Peptides and Proteins: Vol 38","author":"Cryle M. 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