N-(4,7-dihydroxy-2-oxo-8-prop-2-enylchromen-3-yl)benzamide | 1206788-41-1

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 香豆素及其衍生物
• 英文名称: N-(4,7-dihydroxy-2-oxo-8-prop-2-enylchromen-3-yl)benzamide
• CAS: 1206788-41-1
• 化学式: C₁₉H₁₅NO₅
• 分子量: 337.332
• InChiKey: HLNVKTOOYOSMOO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  25
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.05
• 拓扑面积：
  95.9
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  N-(4,7-dihydroxy-2-oxo-2H-chromen-3-yl)benzamide 、 allyl-S-adenosyl homocysteine 在 Streptomyces spheroides DSMZ 40292 Strep-tagged NovO C-methyltransferase 作用下， 以 aq. phosphate buffer 、 二甲基亚砜 为溶剂， 生成 N-(4,7-dihydroxy-2-oxo-8-prop-2-enylchromen-3-yl)benzamide
  参考文献：
  名称：

  Molecular characterization of the C-methyltransferase NovO of Streptomyces spheroides, a valuable enzyme for performing Friedel–Crafts alkylation

  摘要：

  The methyltransferase NovO cloned from Streptomyces spheroides could be heterologously produced as soluble and active enzyme in Escherichia coli. Sequencing of the cloned novO gene revealed differences to the GenBank entry AAF67508.1 resulting in a different amino acid at position 223 (Cys instead of Ser). A generated variant containing a Ser residue at this position, however, resulted in poor ability to express soluble and enzymatically active protein. Characterization of NovO revealed a type I methyltransferase that performs its action as a dimer in solution. Functional elements include the conserved S-adenosyl-L-methionine (SAM) binding site (consensus: E/DXXXGXG) as DLCCGSG (residues 45-51). Mutation analyses of the respective amino acids verified their importance for cofactor binding and enzyme activity. In soluble protein fractions of mutants D45N and G49A the calculated kat values decreased from 2.5 x 10(-2) s(-1) of the wild-type protein to 9.7 x 10(-4) s(-1) and 1.2 x 10(-3) s(-1), respectively. A histidine at position 15 was identified as the catalytic base in the methyl transfer reaction. The analysis of purified enzyme preparations showed that the transfer of allyl groups via the SAM analog allyl-SAH occurs with a fourfold increased K-cat of 11 x 10(-3) s(-1) compared to 3.2 x 10(-3) s(-1) for methyl transfer. However, the evolutionary design toward SAM is obvious from the Km value of 0.06 mM compared to 0.22 mM for allyl-SAH. (C) 2012 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2012.03.016

文献信息

• Biocatalytic Friedel-Crafts Alkylation Using Non-natural Cofactors
  作者：Harald Stecher、Martin Tengg、Bernhard J. Ueberbacher、Peter Remler、Helmut Schwab、Herfried Griengl、Mandana Gruber-Khadjawi

  DOI：10.1002/anie.200905095

  日期：2009.12.7

  A novel biocatalytic protocol for CC bond formation is described and is an equivalent to Friedel–Crafts alkylation. S‐Adenosyl‐L‐methionine (SAM), the major methyl donor for biological methylation catalyzed by methyltransferases (Mtases), can perform alkylations (see scheme). These enzymes can accept non‐natural cofactors and transfer functionalities other than methyl onto aromatic substrates.

  描述了一种新颖的CC键形成的生物催化方案，该方案等同于Friedel-Crafts烷基化。S-腺苷-L-蛋氨酸（SAM）是甲基转移酶（Mtases）催化的生物甲基化的主要甲基供体，可以进行烷基化（请参阅方案）。这些酶可以接受非天然的辅助因子，并且可以将甲基以外的其他功能转移到芳香族底物上。