YC-17 | 36826-66-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: YC-17
• 英文别名: 10-deoxymethymycin；(3R,4S,5S,7R,9E,11R,12R)-4-[(2S,3R,4S,6R)-4-(dimethylamino)-3-hydroxy-6-methyloxan-2-yl]oxy-12-ethyl-3,5,7,11-tetramethyl-1-oxacyclododec-9-ene-2,8-dione
• CAS: 36826-66-1
• 化学式: C₂₅H₄₃NO₆
• 分子量: 453.62
• InChiKey: DZGHWPQKGWXOHD-NHLONWFASA-N

物化性质

• 沸点：
  599.0±50.0 °C(Predicted)
• 密度：
  1.09±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  32
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.84
• 拓扑面积：
  85.3
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  YC-17 在 potassium dihydrogenphosphate 、 乙二胺四乙酸 、 还原型辅酶II(NADPH)四钠盐 作用下， 生成 (2R,3S,7R,9S,10S,11R)-10-[(2S,3R,4S,6R)-4-二甲基氨基-3-羟基-6-甲基-四氢吡喃-2-基]氧基-2-乙基-3-羟基-3,7,9,11-四甲基-1-氧杂环十二碳-4-烯-6,12-二酮
  参考文献：
  名称：

  Macrolide biosynthesis: A single cytochrome P450, PicK, is responsible for the hydroxylations that generate methymycin, neomethymycin, and picromycin in Streptomyces venezuelae

  摘要：

  The final step in the biosynthesis of methymycin, neomethymycin, and picromycin is an hydroxylation, shown to be carried out by the cytochrome P-450 monooxygenase, PicK. Direct comparison of the relative k(cat)/K-m values for the two substrates, YC-17 and narbomycin, showed a threefold rate preference of picK for narbomycin. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00553-8
• 作为产物：
  描述：

  10-去氧微甘菊内酯 、 TDP α-D-desosamine 在 DesVII-C-His₆ 、 DesVIII 、 bovine serum albumin 作用下， 以 phosphate buffer 、 乙醇 、 甘油 为溶剂， 反应 18.0h， 生成 YC-17
  参考文献：
  名称：

  线性糖苷配基是甲基霉素生物合成中糖基转移酶 DesVII 的底物：分析和启示

  摘要：

  大环内酯类抗生素的两个基本结构成分是聚酮苷元和附加糖。苷元的形成由聚酮合酶 (PKS) 催化，糖基化由适当的糖基转移酶催化。虽然已经表明糖基化发生在环状苷元从 PKS 释放后，但尚不清楚与酰基载体蛋白 (ACP) 结合的线性聚酮链是否也可以被相应的糖基转移酶处理。为了探索这种可能性，以线性形式化学合成了作为 N-乙酰半胱胺 (NAC) 硫酯的糖苷配基 10-脱氧甲炔内酯，它是甲霉素和新甲霉素的前体。随后在专用糖基转移酶 DesVII 和激活剂 DesVIII 存在下与 TDP-d-desosamine 孵育，产生极性更强的产物，其高分辨率质量与预期的糖基化产物一致。该研究首次证明大环内酯糖基转移酶也可以识别和加工其大环内酯底物的线性前体，但活性降低但可测量。

  DOI：

  10.1021/ja058433v

文献信息

• SELECTIVE OXIDATION OF C-H BONDS OF MODIFIED SUBSTRATES BY P450 MONOOXYGENASE
  申请人：Li Shengying

  公开号：US20120190635A1

  公开（公告）日：2012-07-26

  The present invention provides regio- and stereoselective oxidation of unactivated C—H bonds using an engineered mutant cytochrome P450 monooxygenase and an engineered substrate.

  本发明提供了使用经过改造的突变型细胞色素P450单氧酶和经过改造的底物对非活化的C-H键进行区域和立体选择性氧化的方法。
• Engineering and Analysis of a Self-Sufficient Biosynthetic Cytochrome P450 PikC Fused to the RhFRED Reductase Domain
  作者：Shengying Li、Larissa M. Podust、David H. Sherman

  DOI：10.1021/ja075842d

  日期：2007.10.1

  first in vitro characterization of a bacterial biosynthetic cytochrome P450 PikC fused to a heterologous reductase domain RhFRED that demonstrates single-component self-sufficiency. This novel fusion system not only produces a more active and effective biocatalyst but also suggests a general design for a universal reductase to generate diverse self-sufficient fusions for functional identification or industrial

  细胞色素 P450 酶介导生物系统中的重要氧化过程，包括区域和立体特异性羟基化和环氧化反应。这些生物分子对单独氧化还原伙伴的固有要求极大地限制了它们在生物技术中的应用。为了应对这一挑战，已利用具有共价融合氧化还原伙伴的天然和/或生物工程自给自足 P450 系统来利用其催化能力。在这项研究中，我们描述了细菌生物合成细胞色素 P450 PikC 与异源还原酶结构域 RhFRED 融合的首次体外表征，该结构域展示了单组分自给自足。
• Recombinant narbonolide polyketide synthase
  申请人：——

  公开号：US20030104597A1

  公开（公告）日：2003-06-05

  Recombinant DNA compounds that encode all or a portion of the narbonolide polyketide synthase are used to express recombinant polyketide synthase genes in host cells for the production of narbonolide, narbonolide derivatives, and polyketides that are useful as antibiotics and as intermediates in the synthesis of compounds with pharmaceutical value.

  编码全部或部分纳碳内酯多酮合成酶的重组 DNA 化合物可用于在宿主细胞中表达重组多酮合成酶基因，以生产纳碳内酯、纳碳内酯衍生物和多酮类化合物，这些化合物可用作抗生素和合成具有药用价值的化合物的中间体。
• Directing Group-Controlled Regioselectivity in an Enzymatic C–H Bond Oxygenation
  作者：Solymar Negretti、Alison R. H. Narayan、Karoline C. Chiou、Petrea M. Kells、Jessica L. Stachowski、Douglas A. Hansen、Larissa M. Podust、John Montgomery、David H. Sherman

  DOI：10.1021/ja5016052

  日期：2014.4.2

  Highly regioselective remote hydroxylation of a natural product scaffold is demonstrated by exploiting the anchoring mechanism of the biosynthetic P450 monooxygenase PikC(D50N)-RhFRED. Previous studies have revealed structural and biochemical evidence for the role of a salt bridge between the desosamine N,N-dimethylamino functionality of the natural substrate YC-17 and carboxylate residues within the active site of the enzyme, and selectivity in subsequent C-H bond functionalization. In the present study, a substrate-engineering approach was conducted that involves replacing desosamine with varied synthetic N,N-dimethylamino anchoring groups. We then determined their ability to mediate enzymatic total turnover numbers approaching or exceeding that of the natural sugar, while enabling ready introduction and removal of these amino anchoring groups from the substrate. The data establish that the size, stereochemistry, and rigidity of the anchoring group influence the regioselectivity of enzymatic hydroxylation. The natural anchoring group desosamine affords a 1:1 mixture of regioisomers, while synthetic anchors shift YC-17 analogue C-10/C-12 hydroxylation from 20:1 to 1:4. The work demonstrates the utility of substrate engineering as an orthogonal approach to protein engineering for modulation of regioselective C-H functionalization in biocatalysis.
• US6902913B2
  申请人：——

  公开号：US6902913B2

  公开（公告）日：2005-06-07