nicotinamide cytosine dinucleotide | 5624-34-0

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - （5'->5'）-二核苷酸
• 英文名称: nicotinamide cytosine dinucleotide
• CAS: 5624-34-0
• 化学式: C₂₀H₂₇N₅O₁₅P₂
• 分子量: 639.406
• InChiKey: CRWNYXSXULHVKY-CASWGKKBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.23
• 重原子数：
  42.0
• 可旋转键数：
  11.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  312.38
• 氢给体数：
  7.0
• 氢受体数：
  17.0

反应信息

• 作为产物：
  描述：

  β-烟酰胺单核苷酸 、 5'-胞苷酸 在 N-甲基咪唑 、 三苯基膦 作用下， 以 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 1.08h， 以11%的产率得到nicotinamide cytosine dinucleotide
  参考文献：
  名称：

  Creation of Bioorthogonal Redox Systems Depending on Nicotinamide Flucytosine Dinucleotide

  摘要：

  Many enzymes catalyzing biological redox chemistry depend on the omnipresent cofactor, nicotinamide adenine dinucleotide (NAD). NAD is also involved in various nonredox processes. It remains challenging to disconnect one particular NAD-dependent reaction from all others. Here we present a bioorthogonal system that catalyzes the oxidative decarboxylation of L-malate with a dedicated abiotic cofactor, nicotinamide flucytosine dinucleotide (NFCD). By screening the multisite saturated mutagenesis libraries of the NAD-dependent malic enzyme (ME), we identified the mutant ME-L310R/Q401C, which showed excellent activity with NFCD, yet marginal activity with NAD. We found that another synthetic cofactor, nicotinamide cytosine dinucleotide (NCD), also displayed similar activity with the ME mutants. Inspired by these observations, we mutated D-lactate dehydrogenase (DLDH) and malate dehydrogenase (MDH) to DLDH-V152R and MDH-L6R, respectively, and both mutants showed fully active with NFCD. When coupled with DLDH-V152R, ME-L310R/Q401C required only a catalytic amount of NFCD to convert L-malate. Our results opened the window to engineer bioorthogonal redox systems for a wide variety of applications in systems biology and synthetic biology.

  DOI：

  10.1021/ja2074032

文献信息

• Gram-scale biocatalytic preparation of the non-natural cofactor nicotinamide cytosine dinucleotide
  作者：Li Wan、Xueying Wang、Yinghan Hu、Qing Li、Zongbao K. Zhao

  DOI：10.1016/j.tetlet.2021.153568

  日期：2022.1

  A simple and fast method of preparation of non-natural nicotinamide adenine dinucleotide (NAD) analog nicotinamide cytosine dinucleotide (NCD) was developed. NCD synthetase (NcdS-1) was developed from nicotinic acid mononucleotide adenylyltransferase (NadD) with higher catalytic efficiency towards nicotinamide mononucleotide (NMN) and cytidine triphosphate (CTP). Reaction composition was optimized

  开发了一种简单快速的非天然烟酰胺腺嘌呤二核苷酸 (NAD) 类似物烟酰胺胞嘧啶二核苷酸 (NCD) 的制备方法。NCD 合成酶 (NcdS-1) 由烟酸单核苷酸腺苷酸转移酶 (NADD) 发展而来，对烟酰胺单核苷酸 (NMN) 和胞苷三磷酸 (CTP) 具有更高的催化效率。使用来自大肠杆菌的无机焦磷酸酶 (PPase) 优化反应组成，以实现底物的接近定量转化。确定了可扩展的纯化程序，以实现 96% 纯度的快速 4.19 g NCD 制备。