Structure of OxyAtei: completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade
Structure of OxyAtei: completing our picture of the glycopeptide antibiotic producing Cytochrome P450 cascade
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DOI：
10.1002/1873-3468.12081
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发表时间：
2016-02-01
期刊：
影响因子：
3.5
通讯作者：
Cryle, Max J.
中科院分区：
文献类型：
--
作者：
Haslinger, Kristina;Cryle, Max J.
糖肽抗生素前体的环化在细胞色素P450酶催化下分三步或四步进行。迄今为止，这些酶中的三种已被结构表征，其中第二种酶沿着途径OxyA逃避结构分析。我们现在能够呈现参与替考拉宁生物合成的OxyA（tei）的结构-最近被证明是第一个活性OxyA同系物的相同酶。尽管替考拉宁前体具有疏水性，但OxyAtei的极性活性位点及其对某些唑类抑制剂的亲和力表明其偏好具有极性修饰的底物。
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 OxyAtei and its affinity for certain azole inhibitors hint at its preference for substrates with polar decorations.