(S)-4-[(S)-2-Acetylamino-3-(3-formyl-4-phosphonooxy-phenyl)-propionylamino]-4-dipentylcarbamoyl-butyric acid

• 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: (S)-4-[(S)-2-Acetylamino-3-(3-formyl-4-phosphonooxy-phenyl)-propionylamino]-4-dipentylcarbamoyl-butyric acid
• 英文别名: (4S)-4-[[(2S)-2-acetamido-3-(3-formyl-4-phosphonooxyphenyl)propanoyl]amino]-5-(dipentylamino)-5-oxopentanoic acid
• 化学式: C₂₇H₄₂N₃O₁₀P
• 分子量: 599.618
• InChiKey: YVZSSHVXIUOJTL-GOTSBHOMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  41
• 可旋转键数：
  20
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  200
• 氢给体数：
  5
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  (S)-4-[(S)-2-Acetylamino-3-(4-hydroxy-phenyl)-propionylamino]-4-dipentylcarbamoyl-butyric acid tert-butyl ester 在 钯 二甲基硫 、 mercury(II) diacetate 、 四丁基氟化铵 、 碘 、 sodium hydride 、 臭氧 、 三乙胺 、 三氟乙酸 作用下， 生成 (S)-4-[(S)-2-Acetylamino-3-(3-formyl-4-phosphonooxy-phenyl)-propionylamino]-4-dipentylcarbamoyl-butyric acid
  参考文献：
  名称：

  The formation of a covalent complex between a dipeptide ligand and the src SH2 domain

  摘要：

  The X-ray crystal structure of the src SH2 domain revealed the presence of a thiol residue (Cys 188) located proximal to the phosphotyrosine portion of a dipeptide ligand. An aldehyde bearing ligand (1) was designed to position an electrophilic carbonyl group in the vicinity of the thiol. X-ray crystallographic and NMR examination of the complex formed between (1) and the src SH2 domain revealed a hemithioacetal formed by addition of the thiol to the aldehyde group with an additional stabilizing hydrogen bond between the acetal hydroxyl and a backbone carbonyl. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(98)00195-4

文献信息

• The formation of a covalent complex between a dipeptide ligand and the src SH2 domain
  作者：Krystal J. Alligood、Paul S. Charifson、Renae Crosby、Thomas G. Consler、Paul L. Feldman、Robert T. Gampe、Tona M. Gilmer、Steven R. Jordan、Mark W. Milstead、Christopher Mohr、Michael R. Peel、Warren Rocque、Marc Rodriguez、David W. Rusnak、Lisa M. Shewchuk、Daniel D. Sternbach

  DOI：10.1016/s0960-894x(98)00195-4

  日期：1998.5

  The X-ray crystal structure of the src SH2 domain revealed the presence of a thiol residue (Cys 188) located proximal to the phosphotyrosine portion of a dipeptide ligand. An aldehyde bearing ligand (1) was designed to position an electrophilic carbonyl group in the vicinity of the thiol. X-ray crystallographic and NMR examination of the complex formed between (1) and the src SH2 domain revealed a hemithioacetal formed by addition of the thiol to the aldehyde group with an additional stabilizing hydrogen bond between the acetal hydroxyl and a backbone carbonyl. (C) 1998 Elsevier Science Ltd. All rights reserved.