(S)-N-苯基-2-甲基琥珀酰亚胺 | 1026093-55-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯烷类
• 中文名称: (S)-N-苯基-2-甲基琥珀酰亚胺
• 英文名称: (S)-N-phenyl-2-methylsuccinimide
• 英文别名: (3S)-3-methyl-1-phenylpyrrolidine-2,5-dione
• CAS: 1026093-55-9
• 化学式: C₁₁H₁₁NO₂
• 分子量: 189.214
• InChiKey: FHORXLYGTFRULY-QMMMGPOBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  14
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  37.4
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  (S)-methylsuccinic anhydride 在 乙酰氯 、 苯 作用下， 生成 (S)-N-苯基-2-甲基琥珀酰亚胺
  参考文献：
  名称：

  Optically Active Mono-substituted Succinic Acids and Derivatives

  摘要：

  DOI：

  10.1021/ja01866a053

文献信息

• The Substrate Spectra of Pentaerythritol Tetranitrate Reductase, Morphinone Reductase,<i>N</i>-Ethylmaleimide Reductase and Estrogen-Binding Protein in the Asymmetric Bioreduction of Activated Alkenes
  作者：Nicole J. Mueller、Clemens Stueckler、Bernhard Hauer、Nina Baudendistel、Hazel Housden、Neil C. Bruce、Kurt Faber

  DOI：10.1002/adsc.200900832

  日期：2010.2.15

  yellow enzyme (OYE) family, pentaerythritol tetranitrate (PETNR) reductase, N-ethylmaleimide reductase (NEMR), morphinone reductase (MorR) and estrogen-binding protein (EBP1), exhibited a broad substrate tolerance by accepting conjugated enals, enones, imides, dicarboxylic acids and esters, as well as a nitroalkene and therefore can be employed for the asymmetric bioreduction of carbon-carbon double (CC)

  古老的黄色酶（OYE）家族的四种黄素蛋白，季戊四醇四硝酸酯（PETNR）还原酶，N-乙基马来酰亚胺还原酶（NEMR），吗啡酮还原酶（MorR）和雌激素结合蛋白（EBP1）通过接受缀合的烯醛表现出广泛的底物耐受性，烯酮，酰亚胺，二羧酸和酯，以及硝基烯烃，因此可用于碳-碳双键（CC）的不对称生物还原。特别地，与先前研究的OYE相比，吗啡酮还原酶和雌激素结合蛋白通常表现出互补的立体化学偏好。
• Asymmetric Bioreduction of Alkenes Using Ene–Reductases YersER and KYE1 and Effects of Organic Solvents
  作者：Yanto Yanto、Christoph K. Winkler、Stephanie Lohr、Mélanie Hall、Kurt Faber、Andreas S. Bommarius

  DOI：10.1021/ol200394p

  日期：2011.5.20

  activated alkenes by KYE1 from Kluyveromyces lactis and Yers-ER from Yersinia bercovieri, two ene–reductases from the Old Yellow Enzyme family, showed a broad substrate spectrum with a moderate to excellent degree of stereoselectivity. Both substrate- and enzyme-based stereocontrols were observed to furnish opposite stereoisomeric products. The effects of organic solvents on enzyme activity and stereoselectivity

  乳酸克鲁维酵母（Kluyveromyces lactis）的KYE1和伯氏耶尔森氏菌（Yersinia bercovieri）的耶尔-ER（Yersinia bercovieri）的耶尔-ER（Kye1）的不对称反式生物还原，显示了较宽的底物谱，具有中等至极好的立体选择性。观察到基于底物和基于酶的立体对照均提供相反的立体异构产物。这项研究概述了有机溶剂对酶活性和立体选择性的影响，其中显示了即使在高有机溶剂含量下，两相系统己烷和甲苯也能维持生物还原效率。
• A Site-Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity
  作者：Helen S. Toogood、Anna Fryszkowska、Martyn Hulley、Michiyo Sakuma、David Mansell、Gill M. Stephens、John M. Gardiner、Nigel S. Scrutton

  DOI：10.1002/cbic.201000662

  日期：2011.3.21

  Divergent evolution: A site‐saturation study of PETN reductase was performed at conserved substrate binding residues H181 and H184. These residues were shown to dramatically alter the ratio of alkene versus nitro‐group reduction in favour of oxime by‐product formation, as summarised in the picture.

  发散进化：在保守的底物结合残基 H181 和 H184 处进行了 PETN 还原酶的位点饱和研究。如图所示，这些残留物显着改变了烯烃与硝基还原的比例，有利于肟副产物的形成。
• Two “classical” Old Yellow Enzymes from Chryseobacterium sp. CA49: Broad substrate specificity of Chr-OYE1 and limited activity of Chr-OYE2
  作者：Xiao-Qiong Pei、Meng-Yu Xu、Zhong-Liu Wu

  DOI：10.1016/j.molcatb.2015.11.008

  日期：2016.1

  Two putative Old Yellow Enzyme (OYE) homologues, Chr-OYE1 and Chr-OYE2, were identified from the genome of Chryseobacterium sp. CA49 as new members of the "classical" subfamily. Chr-OYE1 and Chr-OYE2 were most closely related to the SYE4 from Shewanella oneidensis and NerA from Agrobacterium radiobacter with 41% and 45% identity, respectively. Both enzymes were expressed in Escherichia coli in soluble form, but their catalytic abilities as ene-reductases were quite different. Among the 19 substrate tested, Chr-OYE1 could catalyze the reduction of 18 of them including an ynone with excellent stereos electivity for several prochiral ones, and its specific activity was roughly 1100-fold high than Chr-OYE2, which only catalyzed 3 of the substrates. After restoring the conserved tyrosine, Chr-OYE2 remained the same substrate spectrum, but showed significantly enhanced activity and stereoselectivity. (C) 2015 Elsevier B.V. All rights reserved.