S-(2-acetamidoethyl) (S)-3-hydroxybutanethioate | 220654-32-0

• 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: S-(2-acetamidoethyl) (S)-3-hydroxybutanethioate
• 英文别名: 3S-Hydroxybutyryl-S-N-acetyl cysteamine；S-(2-acetamidoethyl) (3S)-3-hydroxybutanethioate
• CAS: 220654-32-0
• 化学式: C₈H₁₅NO₃S
• 分子量: 205.278
• InChiKey: ZVRHLXCHWBCWPM-LURJTMIESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  91.7
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  以 四氢呋喃 为溶剂， 反应 72.0h， 以63%的产率得到S-(2-acetamidoethyl) (S)-3-hydroxybutanethioate
  参考文献：
  名称：

  In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase

  摘要：

  “一种真菌高度还原型多酮合成酶的分离脱水酶（DH）域的底物选择性与哺乳动物脂肪酸合成酶密切相关。”

  DOI：

  10.1039/c6cc10172k

文献信息

• Seven-enzyme <i>in vitro</i> cascade to (3<i>R</i>)-3-hydroxybutyryl-CoA
  作者：Luis E. Valencia、Zhicheng Zhang、Alexis J. Cepeda、Adrian T. Keatinge-Clay

  DOI：10.1039/c8ob02858c

  日期：——

  convert feedstock chemicals like acetate into valuable chiral products such as (R)-3-hydroxybutyrate are in demand. Here, seven enzymes (CoaA, CoaD, CoaE, ACS, BktB, PhaB, and GDH) are employed in a one-pot, in vitro, biocatalytic synthesis of (3R)-3-hydroxybutyryl-CoA, which was readily isolated. This platform generates not only chiral diketide building blocks but also desirable CoA derivatives.

  需要经济和环境友好的途径，以将原料化学品如乙酸盐转化为有价值的手性产物，如（R）-3-羟基丁酸酯。在这里，一锅，体外，生物催化合成（3 R）-3-羟基丁酰-CoA的七个酶（CoaA，CoaD，CoaE，ACS，BktB，PhaB和GDH）被容易地分离出。该平台不仅可以生成手性二酮化合物，而且还可以生成所需的CoA衍生物。
• The substrate scope of dehydratases in antibiotic biosynthesis and their application in kinetic resolutions
  作者：Zhiyong Yin、Daniel Bär、Bertolt Gust、Jeroen S. Dickschat

  DOI：10.1039/d2ob01879a

  日期：——

  The dehydratase BorDH2 from borrelidin biosynthesis was found to have a wide substrate tolerance in the dehydration of 3D alcohols and was applied in kinetic resolutions.

  从硼菌素生物合成中发现的脱水酶BorDH2在3D醇的脱水中具有广泛的底物耐受性，并应用于动力学分辨率中。
• Enediyne Polyketide Synthases Stereoselectively Reduce the β-Ketoacyl Intermediates to β-<scp>d</scp>-Hydroxyacyl Intermediates in Enediyne Core Biosynthesis
  作者：Hui-Ming Ge、Tingting Huang、Jeffrey D. Rudolf、Jeremy R. Lohman、Sheng-Xiong Huang、Xun Guo、Ben Shen

  DOI：10.1021/ol501767v

  日期：2014.8.1

  PKSE biosynthesizes an enediyne core precursor from decarboxylative condensation of eight malonyl-CoAs. The KR domain of PKSE is responsible for iterative β-ketoreduction in each round of polyketide chain elongation. KRs from selected PKSEs were investigated in vitro with β-ketoacyl-SNACs as substrate mimics. Each of the KRs reduced the β-ketoacyl-SNACs stereoselectively, all affording the corresponding β-D-hydroxyacyl-SNACs, and the catalytic efficiencies (k(cat)/K(M)) of the KRs increased significantly as the chain length of the β-ketoacyl-SNAC substrate increases.
• In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase
  作者：Emma Liddle、Alan Scott、Li-Chen Han、David Ivison、Thomas J. Simpson、Christine L. Willis、Russell J. Cox

  DOI：10.1039/c6cc10172k

  日期：——

  The substrate selectivity of the isolated dehydratase (DH) domain of a fungal highly-reducing polyketide synthase is closely related to that of mammalian fatty acid synthase.

  “一种真菌高度还原型多酮合成酶的分离脱水酶（DH）域的底物选择性与哺乳动物脂肪酸合成酶密切相关。”