ethyl 4-(1H-pyrazol-1-yl)propanoate | 143426-72-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑类
• 英文名称: ethyl 4-(1H-pyrazol-1-yl)propanoate
• 英文别名: ethyl 3-<4-(1-pyrazolyl)phenyl>propanoate；ethyl 3-(4-pyrazol-1-ylphenyl)propanoate
• CAS: 143426-72-6
• 化学式: C₁₄H₁₆N₂O₂
• 分子量: 244.293
• InChiKey: DRNRZNYWMFRARD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.37
• 重原子数：
  18.0
• 可旋转键数：
  5.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  44.12
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  ethyl 4-(1H-pyrazol-1-yl)propanoate 在 sodium hydroxide 作用下， 生成 3-<4-(1-pyrazolyl)phenyl>propanoic acid
  参考文献：
  名称：

  非对映选择性钯（0）催化的手性N-酰基氧杂唑烷酮的烯醇锂的反应。2-取代的（E）-4-亚烷基戊二酸二酯的不对称合成

  摘要：

  钯（0）烯醇化物锂催化的的反应1的Ñ与3-乙酰氧基-2- methylenealkanoates -acyloxazolidinones 2，通过容易地制备DABCO催化对应与丙烯酸酯的醛的联接，非对映选择性进行，并且区域选择性，得到手性ñ - [（E）-4-烷氧基羰基-4-戊烯基]恶唑烷酮3，金属肽酶抑制剂的有用中间体。

  DOI：

  10.1016/0040-4039(95)01043-h
• 作为产物：
  描述：

  4-(1-吡唑基)苯甲酸甲酯 在 palladium on activated charcoal sodium tetrahydroborate 、 氢气 、 potassium carbonate 、 pyridinium chlorochromate 、 calcium chloride 作用下， 以 四氢呋喃 、 乙醇 、 二氯甲烷 、 乙酸乙酯 为溶剂， 25.0~70.0 ℃ 、405.3 kPa 条件下， 反应 7.5h， 生成 ethyl 4-(1H-pyrazol-1-yl)propanoate
  参考文献：
  名称：

  Aromatic hydrazides as specific inhibitors of bovine serum amine oxidase

  摘要：

  New hydrazides were synthesized in search for specific inhibitors of bovine serum amine oxidase: a series of benzoic and phenylacetic acid hydrazides containing the 1H-imidazol-1-yl or the 1H-imidazol-1-ylmethyl group as (o, m, p)-substituent in the phenyl ring; an analogous series of p-substituted phenylhydrazides with 5 or 6-membered heterocyclic ring as substituent, and a series of similar phenylpropionic hydrazides. The longer and more flexible phenylacetic hydrazides, and to a somewhat lesser extent the phenylpropionic ones, were better specific inhibitors of bovine serum amine oxidase than the benzoic hydrazides, which were also bound by the enzyme with high affinity, but at a slow rate. Derivatives with p- and m -substituents were more reactive than the o-substituted ones. The chemical nature of the substituent was less important than its position in the phenyl ring and the presence of methylene spacers. These data point to the presence of a hydrophobic site at short distance from the protein carbonyl cofactor, so that simultaneous interaction of the 2 ends of the inhibitor molecule can occur at the 2 sites. The presence of the hydrophobic site was confirmed by the capability of some molecule deprived of the hydrazidic group to act as mild inhibitors. All hydrazides were less reactive by 2-3 orders of magnitude towards pig kidney diamine oxidase and FAD-dependent monoamine oxidase from rat brain mitochondria, while the other compounds showed similar inhibition power against all proteins. The specificity for the bovine enzyme seems therefore to be related to the concerted action of the 2 moieties of the inhibitor molecule.

  DOI：

  10.1016/0223-5234(92)90005-l