5-Hydroxyamino-2-furaldehyde semicarbazone | 98135-56-9

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 5-Hydroxyamino-2-furaldehyde semicarbazone
• 英文别名: [[5-(hydroxyamino)furan-2-yl]methylideneamino]urea
• CAS: 98135-56-9
• 化学式: C₆H₈N₄O₃
• 分子量: 184.155
• InChiKey: IABKEDDTDTWWRF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  13
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  113
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  呋喃西林 在 His₆-tagged Staphylococcus saprophyticus DSM 20229/ATCC 15305 nitroreductase 、 [(2S,3R,4R)-5-(7,8-二甲基-2,4-二氧代苯并[g]蝶啶-10-基)-2,3,4-三羟基戊基]磷酸二氢酯 、 还原型辅酶II(NADPH)四钠盐 作用下， 以 二甲基亚砜 为溶剂， 生成 5-Hydroxyamino-2-furaldehyde semicarbazone
  参考文献：
  名称：

  An unusually cold active nitroreductase for prodrug activations

  摘要：

  A set of PCR primers based on the genome sequence were used to clone a gene encoding a hypothetical nitroreductases (named as Ssap-NtrB) from uropathogenic staphylococcus, Staphylococcus saprophyticus strain ATCC 15305, an oxygen insensitive flavoenzyme. Activity studies of the translation product revealed that the nitroreductase catalyses two electron reduction of a nitroaromatic drug of nitrofurazone (NFZ), cancer prodrugs of CB1954 and SN23862 at optimum temperature of 20 degrees C together with retaining its maximum activity considerably at 3 degrees C. The required electrons for such reduction could be supplied by either NADH or NADPH with a small preference for the latter. The gene was engineered for heterologous expression in Escherichia coli, and conditions were found in which the enzyme was produced in a mostly soluble form. The recombinant enzyme was purified to homogeneity and physical, spectral and catalytical properties were determined. The findings lead us to propose that Ssap-NtrB represents a novel nitro reductase with an unusual cold active property, which has not been described previously for prodrug activating enzymes of nitroreductases. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.04.004

文献信息

• Engineering a nicotinamide mononucleotide redox cofactor system for biocatalysis
  作者：William B. Black、Linyue Zhang、Wai Shun Mak、Sarah Maxel、Youtian Cui、Edward King、Bonnie Fong、Alicia Sanchez Martinez、Justin B. Siegel、Han Li

  DOI：10.1038/s41589-019-0402-7

  日期：2020.1

  Biological production of chemicals often requires the use of cellular cofactors, such as nicotinamide adenine dinucleotide phosphate (NADP+). These cofactors are expensive to use in vitro and difficult to control in vivo. We demonstrate the development of a noncanonical redox cofactor system based on nicotinamide mononucleotide (NMN+). The key enzyme in the system is a computationally designed glucose dehydrogenase

  化学品的生物生产通常需要使用细胞辅助因子，例如烟酰胺腺嘌呤二核苷酸磷酸 (NADP+)。这些辅助因子在体外使用起来很昂贵并且在体内难以控制。我们展示了基于烟酰胺单核苷酸（NMN+）的非规范氧化还原辅因子系统的开发。该系统中的关键酶是一种经过计算设计的葡萄糖脱氢酶，根据明显的酶活性，其辅因子特异性可切换至 NMN+（而非 NADP+）。我们证明，该系统可用于在体外支持多种氧化还原化学反应，具有高总周转数（~39,000），引导大肠杆菌全细胞中的还原能力，特别是从葡萄糖到药物中间体左旋二酮，并维持高代谢中央碳代谢支持生长所需的通量。总体而言，这项工作证明了非经典辅因子在生物催化和代谢途径设计中的有效利用。
• An unusually cold active nitroreductase for prodrug activations
  作者：Ayhan Çelik、Gülden Yetiş

  DOI：10.1016/j.bmc.2012.04.004

  日期：2012.6

  A set of PCR primers based on the genome sequence were used to clone a gene encoding a hypothetical nitroreductases (named as Ssap-NtrB) from uropathogenic staphylococcus, Staphylococcus saprophyticus strain ATCC 15305, an oxygen insensitive flavoenzyme. Activity studies of the translation product revealed that the nitroreductase catalyses two electron reduction of a nitroaromatic drug of nitrofurazone (NFZ), cancer prodrugs of CB1954 and SN23862 at optimum temperature of 20 degrees C together with retaining its maximum activity considerably at 3 degrees C. The required electrons for such reduction could be supplied by either NADH or NADPH with a small preference for the latter. The gene was engineered for heterologous expression in Escherichia coli, and conditions were found in which the enzyme was produced in a mostly soluble form. The recombinant enzyme was purified to homogeneity and physical, spectral and catalytical properties were determined. The findings lead us to propose that Ssap-NtrB represents a novel nitro reductase with an unusual cold active property, which has not been described previously for prodrug activating enzymes of nitroreductases. (C) 2012 Elsevier Ltd. All rights reserved.