Amino-(4-guanidino-phenyl)-acetic acid | 100294-47-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Amino-(4-guanidino-phenyl)-acetic acid
• 英文别名: 2-Amino-2-[4-(diaminomethylideneamino)phenyl]acetic acid
• CAS: 100294-47-1
• 化学式: C₉H₁₂N₄O₂
• 分子量: 208.22
• InChiKey: FKTCUAKAAIDOCJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.2
• 重原子数：
  15
• 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：
  128
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  β-naphthylamide of p-guanidino-DL-phenylglycine hydrochloride 在 phosphate buffer 、 bovine leukocyte aminopeptidase (BL-APase) 作用下， 生成 Amino-(4-guanidino-phenyl)-acetic acid
  参考文献：
  名称：

  .BETA.-Naphthylamides of guanidinophenyl amino acids as substrates of aminopeptidases.

  摘要：

  合成了对-胍基-L-苯丙氨酸（GPA）和对-胍基-DL-苯甘氨酸（GPG）的β-萘甲酰胺，并将其作为牛白细胞氨肽酶（BL-APase）和猪肝氨肽酶 B（PL-APaseB）的底物与 L-精氨酸β-萘甲酰胺（Arg-βNA）进行了比较试验。BL-APase 催化 GPA-βNA 的水解速度与 Arg-βNA 一样快，而 GPG-βNA 的水解速度要慢得多。BL-AP 酶水解 GPA-βNA 的特异性常数（Vmax/Km）略大于水解 Arg-βNA。根据两种 β-萘甲酰胺底物 Km 值的比较，GPA-βNA 侧链中的苯环被认为有助于该底物与该酶特异性侧的结合。在底物浓度高于约 0.1 mM 的范围内，观察到 BL-APase 在水解 GPA-βNA 时存在底物抑制作用。PL-APaseB 不水解 GPA-βNA 也不水解 GPG-βNA，而且它们抑制该酶水解 Arg-βNA。预计 GPA-βNA 将成为研究氨基肽酶结合和催化特异性的有用底物。

  DOI：

  10.1248/cpb.36.1205

文献信息

• FURIN INHIBITORS
  申请人：Smith Robert E.

  公开号：US20090131328A1

  公开（公告）日：2009-05-21

  Inhibitors for the endoprotease furin are provided for the prevention, diagnosis, treatment, and study of human and animal pathologies, which involve furin activity. These pathologies include infections caused by bacteria and virus that exploit host furin activity. These pathologies also include diseases that involve the expression of host proproteins that are processed by furin as a part of growth, development, and maintenance of the host organism including certain cancers of the head and neck.
• US8263563B2
  申请人：——

  公开号：US8263563B2

  公开（公告）日：2012-09-11
• .BETA.-Naphthylamides of guanidinophenyl amino acids as substrates of aminopeptidases.
  作者：HIDEAKI TSUNEMATSU、HIDEKAZU ARATANI、KOICHI MIZUSAKI、YOSHIHIRO HATANAKA、SHUJI KAWATA、MAGOBEI YAMAMOTO、SATORU MAKISUMI

  DOI：10.1248/cpb.36.1205

  日期：——

  β-Naphthylamides of p-guanidino-L-phenylalanine (GPA) and p-guanidino-DL-phenylglycine (GPG) were synthesized and tested as substrates of bovine leukocyte aminopeptidase (BL-APase) and porcine liver aminopeptidase B (PL-APaseB) in comparison with L-arginine β-naphthylamide (Arg-βNA). BL-APase-catalyzed bydrolysis of GPA-βNA proceeded as fast as that of Arg-βNA, while the rate of hydrolysis of GPG-βNA was much slower. The specificity constant (Vmax/Km) for the hydrolysis of GPA-βNA by BL-APase was somewhat larger than that for the hydrolysis of Arg-βNA. The benzene ring in the side chain of GPA-βNA is considered to contribute to the binding of this substrate to the specificity side to this enzyme, based on comparison of the Km values for the two β-naphthylamide substrates. Substrate inhibition was observed with BL-APase in the hydrolysis of GPA-βNA in the substrate concentration range higher than about 0.1 mM. Neither GPA-βNA nor GPG-βNA was hydrolyzed by PL-APaseB and they inhibited the hydrolysis of Arg-βNA by this enzyme. GPA-βNA is expected to be a useful substrate in the study of the binding and catalytic specificities of aminopeptidases.

  合成了对-胍基-L-苯丙氨酸（GPA）和对-胍基-DL-苯甘氨酸（GPG）的β-萘甲酰胺，并将其作为牛白细胞氨肽酶（BL-APase）和猪肝氨肽酶 B（PL-APaseB）的底物与 L-精氨酸β-萘甲酰胺（Arg-βNA）进行了比较试验。BL-APase 催化 GPA-βNA 的水解速度与 Arg-βNA 一样快，而 GPG-βNA 的水解速度要慢得多。BL-AP 酶水解 GPA-βNA 的特异性常数（Vmax/Km）略大于水解 Arg-βNA。根据两种 β-萘甲酰胺底物 Km 值的比较，GPA-βNA 侧链中的苯环被认为有助于该底物与该酶特异性侧的结合。在底物浓度高于约 0.1 mM 的范围内，观察到 BL-APase 在水解 GPA-βNA 时存在底物抑制作用。PL-APaseB 不水解 GPA-βNA 也不水解 GPG-βNA，而且它们抑制该酶水解 Arg-βNA。预计 GPA-βNA 将成为研究氨基肽酶结合和催化特异性的有用底物。