benzyl (S)-(2-((2-((3-(1H-imidazol-4-yl)-1-oxo-1-((4-sulfamoylphenyl)amino)propan-2-yl)amino)-2-oxoethyl)amino)-2-oxoethyl)carbamate | 1011715-99-3

• 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: benzyl (S)-(2-((2-((3-(1H-imidazol-4-yl)-1-oxo-1-((4-sulfamoylphenyl)amino)propan-2-yl)amino)-2-oxoethyl)amino)-2-oxoethyl)carbamate
• CAS: 1011715-99-3
• 化学式: C₂₄H₂₇N₇O₇S
• 分子量: 557.587
• InChiKey: QZHHQWXXQGSODI-FQEVSTJZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.23
• 重原子数：
  39.0
• 可旋转键数：
  12.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  214.47
• 氢给体数：
  6.0
• 氢受体数：
  8.0

反应信息

• 作为反应物：
  描述：

  benzyl (S)-(2-((2-((3-(1H-imidazol-4-yl)-1-oxo-1-((4-sulfamoylphenyl)amino)propan-2-yl)amino)-2-oxoethyl)amino)-2-oxoethyl)carbamate 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 、 乙酸乙酯 为溶剂， 反应 4.0h， 以28 mg的产率得到(2S)-2-[[2-[(2-aminoacetyl)amino]acetyl]amino]-3-(1H-imidazol-5-yl)-N-(4-sulfamoylphenyl)propanamide
  参考文献：
  名称：

  Catalytic Inactivation of Human Carbonic Anhydrase I by a Metallopeptide−Sulfonamide Conjugate is Mediated by Oxidation of Active Site Residues

  摘要：

  Oxidation of active site residues (His and Trp), following catalytic inactivation of human carbonic anhydrase I by a copper-ATCUN conjugate of sulfanilimide, is evidenced by mass spectrometric analysis of tryptic and chymotryptic digest of the modified CA-I. Accordingly, residue oxidation rather than protein cleavage is the demonstrated mods of inactivation. An apparent second-order rate constant, k(2) similar to 7600 M(-1)min(-1), has been determined for catalytic inactivation of CA-I.

  DOI：

  10.1021/ja0778038
• 作为产物：
  描述：

  磺胺 、 苄氧羰基-甘氨酰-甘氨酰-组氨酸 在 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 甲醇 、 水 为溶剂， 以30 mg的产率得到benzyl (S)-(2-((2-((3-(1H-imidazol-4-yl)-1-oxo-1-((4-sulfamoylphenyl)amino)propan-2-yl)amino)-2-oxoethyl)amino)-2-oxoethyl)carbamate
  参考文献：
  名称：

  Catalytic Inactivation of Human Carbonic Anhydrase I by a Metallopeptide−Sulfonamide Conjugate is Mediated by Oxidation of Active Site Residues

  摘要：

  Oxidation of active site residues (His and Trp), following catalytic inactivation of human carbonic anhydrase I by a copper-ATCUN conjugate of sulfanilimide, is evidenced by mass spectrometric analysis of tryptic and chymotryptic digest of the modified CA-I. Accordingly, residue oxidation rather than protein cleavage is the demonstrated mods of inactivation. An apparent second-order rate constant, k(2) similar to 7600 M(-1)min(-1), has been determined for catalytic inactivation of CA-I.

  DOI：

  10.1021/ja0778038