N-(4-nitro-benzoyl)-glycine hydrazide | 139645-87-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N-(4-nitro-benzoyl)-glycine hydrazide
• 英文别名: N-(4-Nitro-benzoyl)-glycin-hydrazid；4-Nitro-benzaminoessigsaeurehydrazid；4-Nitro-hippursaeurehydrazid；N-hydrazinocarbonylmethyl-4-nitrobenzamide；N-(2-hydrazinyl-2-oxoethyl)-4-nitrobenzamide
• CAS: 139645-87-7
• 化学式: C₉H₁₀N₄O₄
• 分子量: 238.203
• InChiKey: QMWADEBSOGTBNZ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  17
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  130
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-(4-nitro-benzoyl)-glycine hydrazide 在 盐酸 、 甲苯 、 铂 、 sodium nitrite 、 三氯氧磷 作用下， 生成 4-(8,9-dimethoxy-5,6-dihydro-imidazo[5,1-a]isoquinolin-3-yl)-aniline
  参考文献：
  名称：

  Kametani; Iida, Yakugaku Zasshi/Journal of the Pharmaceutical Society of Japan, 1950, vol. 70, p. 258

  摘要：

  DOI：
• 作为产物：
  描述：

  2-[(4-硝基苯甲酰基)氨基]乙酸乙酯 在 乙醇 、 一水合肼 作用下， 生成 N-(4-nitro-benzoyl)-glycine hydrazide
  参考文献：
  名称：

  Curtius, Journal fur praktische Chemie (Leipzig 1954), 1916, vol. <2> 94, p. 130

  摘要：

  DOI：

文献信息

• Curtius, Journal fur praktische Chemie (Leipzig 1954), 1916, vol. <2> 94, p. 130
  作者：Curtius

  DOI：——

  日期：——
• Synthesis and antiviral activities of novel acylhydrazone derivatives targeting HIV-1 capsid protein
  作者：Baohe Tian、Meizi He、Shixing Tang、Indira Hewlett、Zhiwu Tan、Jiebo Li、Yinxue Jin、Ming Yang

  DOI：10.1016/j.bmcl.2009.02.116

  日期：2009.4

  HIV-1 capsid protein (CA) plays important roles in the viral replication cycle. A number of acylhydrazone derivatives that act as inhibitors of HIV-1 CA assembly, were designed and synthesized. The synthesized compounds were tested for their antiviral activities and cytotoxicities using CEM cells. Some derivatives also were assayed for their ability to inhibit HIV-1 CA assembly in vitro. Among them, compounds 14f and 14i display the most promising potency with EC50 values of 0.21 and 0.17 mu M, respectively. (C) 2009 Elsevier Ltd. All rights reserved.
• Kametani et al., Yakugaku Zasshi/Journal of the Pharmaceutical Society of Japan, 1951, vol. 71, p. 325,328
  作者：Kametani et al.

  DOI：——

  日期：——
• Inhibitors of Bacterial Cystathionine β-Lyase:  Leads for New Antimicrobial Agents and Probes of Enzyme Structure and Function
  作者：Linda J. Ejim、Jan E. Blanchard、Kalinka P. Koteva、Rachael Sumerfield、Nadine H. Elowe、Jonathan D. Chechetto、Eric D. Brown、Murray S. Junop、Gerard D. Wright

  DOI：10.1021/jm061132r

  日期：2007.2.1

  The biosynthesis of methionine is an attractive antibiotic target given its importance in protein and DNA metabolism and its absence in mammals. We have performed a high-throughput screen of the methionine biosynthesis enzyme cystathionine beta-lyase (CBL) against a library of 50 000 small molecules and have identified several compounds that inhibit CBL enzyme activity in vitro. These hit molecules were of two classes: those that blocked CBL activity with mixed steady-state inhibition and those that covalently interacted with the enzyme at the active site pyridoxal phosphate cofactor with slow-binding inhibition kinetics. We determined the crystal structure of one of the slow-binding inhibitors in complex with CBL and used this structure as a guide in the synthesis of a small, focused library of analogues, some of which had improved enzyme inhibition properties. These studies provide the first lead molecules for antimicrobial agents that target cystathionine beta-lyase in methionine biosynthesis.
• Kametani; Iida, Yakugaku Zasshi/Journal of the Pharmaceutical Society of Japan, 1950, vol. 70, p. 258
  作者：Kametani、Iida

  DOI：——

  日期：——