NSC3198 | 2752-39-8

• 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: NSC3198
• 英文别名: BSBM7；N,N'-bis-phenylacetyl-cystine；N,N'-Bis-phenylacetyl-cystin；Diphenacetyl-cystin；n,n'-Bis(phenylacetyl)cystine；3-[[2-carboxy-2-[(2-phenylacetyl)amino]ethyl]disulfanyl]-2-[(2-phenylacetyl)amino]propanoic acid
• CAS: 2752-39-8
• 化学式: C₂₂H₂₄N₂O₆S₂
• 分子量: 476.574
• InChiKey: DWRCRIMPBCLETK-UHFFFAOYSA-N

物化性质

• 溶解度：
  0.01 M

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  32
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  183
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  NSC3198 在 sodium tetrahydroborate 作用下， 以90%的产率得到N-phenylacetyl-L-cysteine
  参考文献：
  名称：

  Cysteinyl peptide Inhibitors of Bacillus cereus Zinc β-Lactamase

  摘要：

  Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta -lactamase. The pH dependence of pK(i) indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00257-1
• 作为产物：
  描述：

  L-胱氨酸 、 苯乙酰氯 以80%的产率得到NSC3198
  参考文献：
  名称：

  Cysteinyl peptide Inhibitors of Bacillus cereus Zinc β-Lactamase

  摘要：

  Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta -lactamase. The pH dependence of pK(i) indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site. (C) 2001 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0968-0896(00)00257-1

文献信息

• Shiple; Sherwin, Journal of Biological Chemistry, 1923, vol. 55, p. 679,684
  作者：Shiple、Sherwin

  DOI：——

  日期：——
• Cysteinyl peptide Inhibitors of Bacillus cereus Zinc β-Lactamase
  作者：Sakina Bounaga、Moreno Galleni、Andrew P Laws、Michael I Page

  DOI：10.1016/s0968-0896(00)00257-1

  日期：2001.2

  Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta -lactamase. The pH dependence of pK(i) indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site. (C) 2001 Elsevier Science Ltd. All rights reserved.