| 1241842-86-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• CAS: 1241842-86-3
• 化学式: C₁₆H₂₂O₄
• 分子量: 278.348
• InChiKey: SWUBXAGIIIVMCV-ZDUSSCGKSA-N

反应信息

• 作为反应物：
  描述：

  在 水 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 24.0h， 生成 2-benzyl-5-hydroxy-4-oxopentanoic acid
  参考文献：
  名称：

  Optical 2-benzyl-5-hydroxy-4-oxopentanoic acids against carboxypeptidase A: Synthesis, kinetic evaluation and X-ray crystallographic study

  摘要：

  2-Benzyl-5-hydroxy-4-oxopentanoic acid 1 and its enantiomers were designed, synthesized and assayed for inhibitory activity against carboxypeptidase A (CPA, EC 3.4.17.1). To verify the role of the terminal hydroxyl group in 1 binding to CPA, 2-benzyl-5-benzyloxy-4-oxopentanoic acid 2 was also synthesized and evaluated. The inhibition constants show that both L-1 and D-1 were shown to have strong binding affinity with L-1 being more potent than its enantiomer by 165-fold. On the other hand, the inhibition constant of 2 increases 4-fold comparing with that of 1. In order to explore the exact binding mode of the hydroxyacteyl group of 1 to the active site zinc ion of CPA, we have solved the crystal structure of CPA complexed with L-1 up to 1.85 A resolution. In CPA-L-1 complex, the phenyl ring is fitted in the substrate recognition pocket at the S, subsite, and the carboxylate forms bifurcated hydrogen bonds with the guanidinium moiety of Arg-145 and Arg-127 and a hydrogen bond with the phenolic hydroxyl of the down-positioned Tyr-248. The carbonyl oxygen of L-1 does coordinate to the active site zinc ion of CPA as expectedly. Unexpectedly, the terminal hydroxyl group of L-1 is engaged in hydrogen bonding with carbonyl oxygen of Ser-197 instead of coordinating to the active site zinc ion. (C) 2009 Guan Rong Tian. Published by Elsevier B.V. on behalf of Chinese Chemical Society. All fights reserved.

  DOI：

  10.1016/j.cclet.2009.09.005
• 作为产物：
  描述：

  在 sodium formate 作用下， 以 乙醇 为溶剂， 反应 12.0h， 生成
  参考文献：
  名称：

  Optical 2-benzyl-5-hydroxy-4-oxopentanoic acids against carboxypeptidase A: Synthesis, kinetic evaluation and X-ray crystallographic study

  摘要：

  2-Benzyl-5-hydroxy-4-oxopentanoic acid 1 and its enantiomers were designed, synthesized and assayed for inhibitory activity against carboxypeptidase A (CPA, EC 3.4.17.1). To verify the role of the terminal hydroxyl group in 1 binding to CPA, 2-benzyl-5-benzyloxy-4-oxopentanoic acid 2 was also synthesized and evaluated. The inhibition constants show that both L-1 and D-1 were shown to have strong binding affinity with L-1 being more potent than its enantiomer by 165-fold. On the other hand, the inhibition constant of 2 increases 4-fold comparing with that of 1. In order to explore the exact binding mode of the hydroxyacteyl group of 1 to the active site zinc ion of CPA, we have solved the crystal structure of CPA complexed with L-1 up to 1.85 A resolution. In CPA-L-1 complex, the phenyl ring is fitted in the substrate recognition pocket at the S, subsite, and the carboxylate forms bifurcated hydrogen bonds with the guanidinium moiety of Arg-145 and Arg-127 and a hydrogen bond with the phenolic hydroxyl of the down-positioned Tyr-248. The carbonyl oxygen of L-1 does coordinate to the active site zinc ion of CPA as expectedly. Unexpectedly, the terminal hydroxyl group of L-1 is engaged in hydrogen bonding with carbonyl oxygen of Ser-197 instead of coordinating to the active site zinc ion. (C) 2009 Guan Rong Tian. Published by Elsevier B.V. on behalf of Chinese Chemical Society. All fights reserved.

  DOI：

  10.1016/j.cclet.2009.09.005