(R)-10-Hydroxystearate

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (R)-10-Hydroxystearate
• 英文别名: (10R)-10-hydroxyoctadecanoate
• 化学式: C18H35O3-
• 分子量: 299.5
• InChiKey: PAZZVPKITDJCPV-QGZVFWFLSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  7
• 重原子数：
  21
• 可旋转键数：
  15
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.94
• 拓扑面积：
  60.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (R)-10-Hydroxystearate 生成 oleate 、 水
  参考文献：
  名称：

  Oleate Hydratase Catalyzes the Hydration of a Nonactivated Carbon-Carbon Bond

  摘要：

  摘要 油酸水合转化为 10-羟基硬脂酸的过程最初是由一种假单胞菌描述的。 假单胞菌 细胞提取物中。在这期间，该酶从未被详细表征过。在此，我们报告了从伊丽莎白金丝菌（Elizabethkingia menoseptica）中分离出的油酸氢化酶（EC 4.2.1.53）及其特征。 Elizabethkingia meningoseptica .

  DOI：

  10.1128/jb.00306-09

文献信息

• Myosin Cross-reactive Antigen of Streptococcus pyogenes M49 Encodes a Fatty Acid Double Bond Hydratase That Plays a Role in Oleic Acid Detoxification and Bacterial Virulence
  作者：Anton Volkov、Alena Liavonchanka、Olga Kamneva、Tomas Fiedler、Cornelia Goebel、Bernd Kreikemeyer、Ivo Feussner

  DOI：10.1074/jbc.m109.081851

  日期：2010.4

  M49 is a FAD enzyme, which acts as hydratase on (9Z)- and (12Z)-double bonds of C-16, C-18 non-esterified fatty acids. Products are 10-hydroxy and 10,13-dihydroxy fatty acids. Kinetic analysis suggests that FAD rather stabilizes the active conformation of the enzyme and is not directly involved in catalysis. Analysis of S. pyogenes M49 grown in the presence of either oleic or linoleic acid showed that

  肌球蛋白交叉反应抗原 (MCRA) 蛋白家族在从革兰氏阳性菌到革兰氏阴性菌的不同细菌物种中高度保守。除了它们普遍存在之外，关于 MCRA 蛋白的生化和生理功能的知识很少。在这里，我们展示了来自化脓性链球菌 M49 的 MCRA 蛋白是一种 FAD 酶，它充当 C-16、C-18 非酯化脂肪酸的 (9Z)-和 (12Z)-双键的水合酶。产品是10-羟基和10,13-二羟基脂肪酸。动力学分析表明，FAD 更能稳定酶的活性构象，而不直接参与催化。对在油酸或亚油酸存在下生长的化脓性链球菌 M49 的分析表明，10-羟基和 10,13-二羟基衍生物是唯一的产物。没有检测到这些羟基脂肪酸的进一步代谢。水合酶基因的缺失导致对油酸的最小抑制浓度降低了 2 倍，但增加了突变株在全血中的存活率。与野生型相比，对人角质形成细胞的粘附和内化特性降低。基于这些结果，我们得出结论，先前鉴定的 MCRA 蛋白可以归类为碳氧裂解酶家族内的含
• Biochemical characterization and FAD-binding analysis of oleate hydratase from Macrococcus caseolyticus
  作者：Young-Chul Joo、Ki-Woong Jeong、Soo-Jin Yeom、Yeong-Su Kim、Yangmee Kim、Deok-Kun Oh

  DOI：10.1016/j.biochi.2011.12.011

  日期：2012.3

  A putative fatty acid hydratase gene from Macrococcus caseolyticus was cloned and expressed in Escherichia coli. The recombinant enzyme was a 68 kDa dimer with a molecular mass of 136 kDa. The enzyrnatic products formed from fatty acid substrates by the putative enzyme were isolated with high purity (>99%) by solvent fractional crystallization at low temperature. After the identification by GC MS, the purified hydroxy fatty acids were used as standards to quantitatively determine specific activities and kinetic parameters for fatty acids as substrates. Among the fatty acids evaluated, specific activity and catalytic efficiency (k t1Kin) were highest for oleic acid, indicating that the putative fatty acid hydratase was an oleate hydratase. Hydration occurred only for cis-9-double and cis-12-double bonds of unsaturated fatty acids without any trans-configurations. The maximum activity for oleate hydration was observed at pH 6.5 and 25 C with 2% (v/v) ethanol and 0.2 mM FAD. Without FAD, all catalytic activity was abolished. Thus, the oleate hydratase is an FAD-dependent enzyme. The residues G29, G31, S34, E50, and E56, which are conserved in the FAD-binding motif of fatty acid hydratases (GXGXXG((A/S))X((15-21))E(D), were selected by alignment, and the spectral properties and kinetic parameters of their alanine-substituted variants were analyzed. Among the five variants, G29A. G31A, and E56A showed no interaction with FAD and exhibited no activity. These results indicate that G29, G31, and E56 are essential for FAD-binding. Crown Copyright (C) 2011 Published by Elsevier Masson SAS. All rights reserved.
• Niehaus W.G. Jr.; Torkelson A.; Kisic A., J Biol Chem, 1970, 0021-9258, 3790-7
  作者：Niehaus W.G. Jr.、Torkelson A.、Kisic A.、Bednarczyk D.J.、Schroepfer G.J. Jr.

  DOI：——

  日期：——