2-[2-[[(2S)-2-acetamido-4-methylpentanoyl]amino]acetyl]oxyacetic acid | 1410924-56-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 肽模拟物
• 英文名称: 2-[2-[[(2S)-2-acetamido-4-methylpentanoyl]amino]acetyl]oxyacetic acid
• CAS: 1410924-56-9
• 化学式: C₁₂H₂₀N₂O₆
• 分子量: 288.301
• InChiKey: OSYOVGIYSURCJJ-VIFPVBQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  20
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  122
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  乙酰基-亮氨酰-甘氨酸 在 potassium carbonate 、 三氟乙酸 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 生成 2-[2-[[(2S)-2-acetamido-4-methylpentanoyl]amino]acetyl]oxyacetic acid
  参考文献：
  名称：

  Prohormone-substrate peptide sequence recognition by peptidylglycine α-amidating monooxygenase and its reflection in increased glycolate inhibitor potency

  摘要：

  The interactions of nineteen peptide substrates and fifteen analogous peptidomimetic glycolate inhibitors with human peptidylglycine alpha-amidating monooxygenase (PAM) have been investigated. The substrates and inhibitors are the prohormones of calcitonin and oxytocin and their analogues. PAM both secreted into the medium by and extracted from DMS53 small lung carcinoma cells has been studied. The results show that recognition of the prooxytocin and procalcitonin peptide sequences by the enzyme extends more than four and five amino acid residues, respectively, from their C-termini. This substrate sequence recognition is mirrored by increased inhibitor potency with increased peptide length in the glycolate peptidomimetics. Substitution of the C-terminal penultimate glycine and proline residues of prooxytocin and procalcitonin and their analogues with phenylalanine increases the enzyme binding affinity. However, this changes the binding mode from one that depends on peptide sequence recognition to another primarily determined by the phenylalanine moiety, for both the substrates and analogous glycolate inhibitors. Crown Copyright (C) 2012 Published by Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.10.004

文献信息

• Prohormone-substrate peptide sequence recognition by peptidylglycine α-amidating monooxygenase and its reflection in increased glycolate inhibitor potency
  作者：Kelly M. Morris、Feihua Cao、Hideki Onagi、Timothy M. Altamore、Allan B. Gamble、Christopher J. Easton

  DOI：10.1016/j.bmcl.2012.10.004

  日期：2012.12

  The interactions of nineteen peptide substrates and fifteen analogous peptidomimetic glycolate inhibitors with human peptidylglycine alpha-amidating monooxygenase (PAM) have been investigated. The substrates and inhibitors are the prohormones of calcitonin and oxytocin and their analogues. PAM both secreted into the medium by and extracted from DMS53 small lung carcinoma cells has been studied. The results show that recognition of the prooxytocin and procalcitonin peptide sequences by the enzyme extends more than four and five amino acid residues, respectively, from their C-termini. This substrate sequence recognition is mirrored by increased inhibitor potency with increased peptide length in the glycolate peptidomimetics. Substitution of the C-terminal penultimate glycine and proline residues of prooxytocin and procalcitonin and their analogues with phenylalanine increases the enzyme binding affinity. However, this changes the binding mode from one that depends on peptide sequence recognition to another primarily determined by the phenylalanine moiety, for both the substrates and analogous glycolate inhibitors. Crown Copyright (C) 2012 Published by Elsevier Ltd. All rights reserved.