6-羟基-N-甲基肌氨酸 | 68104-57-4

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 中文名称: 6-羟基-N-甲基肌氨酸
• 英文名称: 6-hydroxy-N-methylmyosmine
• 英文别名: 5-(1-methyl-2,3-dihydropyrrol-5-yl)-1H-pyridin-2-one
• CAS: 68104-57-4
• 化学式: C₁₀H₁₂N₂O
• 分子量: 176.218
• InChiKey: LWGKCPAYDQWMMS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.4
• 重原子数：
  13
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  32.3
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  (R)-(+)-5-(1-methyl-2-pyrrolidinyl)-2(1H)-pyridone 在 Arthrobacter nicotinovorans 6-hydroxy-D-nicotine oxidase 作用下， 以 aq. buffer 为溶剂， 生成 6-羟基-N-甲基肌氨酸
  参考文献：
  名称：

  Turning a monocovalent flavoprotein into a bicovalent flavoprotein by structure-inspired mutagenesis

  摘要：

  A recently discovered class of bicovalent flavoproteins is an interesting group of enzymes because of their unusual cofactor binding mode, their open active sites and the bulky substrates they can accept. Through a sequence comparison study we have identified a conserved sequence region in bicovalent flavoproteins that is different from monocovalent flavoproteins. Based on this and the available structural information we have designed mutants of the prototype monocovalent flavoprotein, 6-hydroxy-D-nicotine oxidase (6HDNO), in order to introduce a second cofactor-protein linkage. Two amino acid replacements, namely histidine 130 to a cysteine and leucine 138 to a histidine, were sufficient to create a bicovalent 6HDNO. The introduced cysteine forms a covalent bond with FAD as found in natural bicovalent flavoproteins, while the second mutation was found to be essential to facilitate the formation of the cysteinyl linkage. This points to an important role of the introduced histidine in stabilizing a negative charge of the isoalloxazine ring during covalent flavinylation. The His130Cys/Leu138His 6HDNO is still active and shows a higher midpoint redox potential when compared to wild-type 6HDNO. This agrees well with the previous studies that have shown that bicovalent flavoenzymes have extremely high redox potentials (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.05.051

文献信息

• Turning a monocovalent flavoprotein into a bicovalent flavoprotein by structure-inspired mutagenesis
  作者：Malgorzata M. Kopacz、Marco W. Fraaije

  DOI：10.1016/j.bmc.2014.05.051

  日期：2014.10

  A recently discovered class of bicovalent flavoproteins is an interesting group of enzymes because of their unusual cofactor binding mode, their open active sites and the bulky substrates they can accept. Through a sequence comparison study we have identified a conserved sequence region in bicovalent flavoproteins that is different from monocovalent flavoproteins. Based on this and the available structural information we have designed mutants of the prototype monocovalent flavoprotein, 6-hydroxy-D-nicotine oxidase (6HDNO), in order to introduce a second cofactor-protein linkage. Two amino acid replacements, namely histidine 130 to a cysteine and leucine 138 to a histidine, were sufficient to create a bicovalent 6HDNO. The introduced cysteine forms a covalent bond with FAD as found in natural bicovalent flavoproteins, while the second mutation was found to be essential to facilitate the formation of the cysteinyl linkage. This points to an important role of the introduced histidine in stabilizing a negative charge of the isoalloxazine ring during covalent flavinylation. The His130Cys/Leu138His 6HDNO is still active and shows a higher midpoint redox potential when compared to wild-type 6HDNO. This agrees well with the previous studies that have shown that bicovalent flavoenzymes have extremely high redox potentials (C) 2014 Elsevier Ltd. All rights reserved.