2-octyl 2-methyl-3-oxobutyrate | 167226-03-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: 2-octyl 2-methyl-3-oxobutyrate
• 英文别名: Octan-2-yl 2-methyl-3-oxobutanoate
• CAS: 167226-03-1
• 化学式: C₁₃H₂₄O₃
• 分子量: 228.332
• InChiKey: WETKNTQNTUSMPJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  16
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.85
• 拓扑面积：
  43.4
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-octyl 2-methyl-3-oxobutyrate 在 buffer Mopso 、 YKER-I 、 还原型辅酶II(NADPH)四钠盐 作用下， 以 水 为溶剂， 以33%的产率得到2-octyl 3-hydroxy-2-methylbutyrate
  参考文献：
  名称：

  Reduction of β-Keto Esters with a Reductase: Construction of Plural Stereocenters Remote from the Reaction Center

  摘要：

  The reduction of sec-alkyl 2-methyl-3-oxobutyrate with a keto ester reductase from bakers' yeast (YKER-I) is accompanied by simultaneous dynamic and static resolution of chiral centers affording the corresponding (2R,3S,1'R)-hydroxy esters preferentially Thus, the enzyme discriminates three chiral centers simultaneously in high stereoselectivity producing useful chiral building blocks. To study the effect of the alcohol moiety which is located at a remote position from the reaction center, upon the interaction between the enzyme and a substrate, steady-state kinetic parameters, K-m and k(cat), of YKER-I for each (1'R)- and (1'S)-substrate have been determined. The results reveal that the stereochemistry at the alcohol moiety affects K-m rather than k(cat). (C) 1999 Academic Press.

  DOI：

  10.1006/bioo.1998.1106
• 作为产物：
  描述：

  双乙烯酮 、 仲辛醇 、 碘甲烷 在 三乙胺 、 四甲基胍 作用下， 生成 2-octyl 2-methyl-3-oxobutyrate
  参考文献：
  名称：

  Reduction of β-Keto Esters with a Reductase: Construction of Plural Stereocenters Remote from the Reaction Center

  摘要：

  The reduction of sec-alkyl 2-methyl-3-oxobutyrate with a keto ester reductase from bakers' yeast (YKER-I) is accompanied by simultaneous dynamic and static resolution of chiral centers affording the corresponding (2R,3S,1'R)-hydroxy esters preferentially Thus, the enzyme discriminates three chiral centers simultaneously in high stereoselectivity producing useful chiral building blocks. To study the effect of the alcohol moiety which is located at a remote position from the reaction center, upon the interaction between the enzyme and a substrate, steady-state kinetic parameters, K-m and k(cat), of YKER-I for each (1'R)- and (1'S)-substrate have been determined. The results reveal that the stereochemistry at the alcohol moiety affects K-m rather than k(cat). (C) 1999 Academic Press.

  DOI：

  10.1006/bioo.1998.1106

文献信息

• Introduction of plural asymmetric centers by a β-keto ester reductase from baker's yeast
  作者：Yasushi Kawai、Kouichi Hida、Kaoru Nakamura、Atsuyoshi Ohno

  DOI：10.1016/0040-4039(94)02260-i

  日期：1995.1

  A β-keto ester reductase from baker's yeast catalyzes asymmetric reduction accompanied by simultaneous kinetic resolution of dynamic and dtatic optically active centers. The reduction of 1′-arylethyl 2-methyl-3-oxobutanoates mediated by this enzyme affords the corresponding (1′R)-1′-arylethyl(2R,3S)-3-hydroxy-2-methylbutanoates with excellent stereoselectivity.

  面包酵母中的β-酮酯还原酶催化不对称还原，并同时动态拆分动态和dtatic光学活性中心。的1'-芳基乙基2-甲基-3- oxobutanoates由该酶介导的还原，得到相应的（1' - [R）-1'-芳基乙基（2 - [R，3小号）-3-羟基-2- methylbutanoates具有优异的立体选择性。