tert-butyl N-[(2R)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methylsulfinyl-1-oxopropan-2-yl]carbamate | 211679-66-2

• 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: tert-butyl N-[(2R)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methylsulfinyl-1-oxopropan-2-yl]carbamate
• CAS: 211679-66-2
• 化学式: C₁₉H₃₆N₄O₇S
• 分子量: 464.583
• InChiKey: FGMPDAJGJMBJBH-BUWIUWGBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.8
• 重原子数：
  31
• 可旋转键数：
  13
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  196
• 氢给体数：
  5
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  苯甲酸酐 、 tert-butyl N-[(2R)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methylsulfinyl-1-oxopropan-2-yl]carbamate 在 三乙胺 、 三氟乙酸 作用下， 生成 N-[(2R)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methylsulfinyl-1-oxopropan-2-yl]benzamide
  参考文献：
  名称：

  Synthesis and Evaluation of Tripeptides Containing Asparagine Analogues as Potential Substrates or Inhibitors of Oligosaccharyltransferase

  摘要：

  The amino acids 5-diazo-4-oxo-L-norvaline, 4-oxo-L-norvaline, and (methanesulfinyl)-L-alanine have been incorporated into three separate tripeptides wherein these nonnatural amino acids replace Asn in a known tripeptide substrate of oligosaccharyltransferase. Synthesis of both the diazoketone- and sulfoxide-containing peptides involved functionalization of the appropriate side chain after peptide assembly, whereas synthesis of the methyl ketone-containing peptide was effected by synthesis of the protected amino acid followed by its incorporation into the desired tripeptide. None of the three synthetic tripeptides showed activity as substrates, nor were they potent inhibitors of oligosaccharyltransferase at concentrations that were 10-35 times the K-m for the corresponding Asn-containing tripeptide substrate. NMR analysis in DMSO-d(6) showed that the diazoketone and methyl ketone peptides adopt the "Asx-turn" conformation, which has been postulated to be crucial for substrate binding. Furthermore, a nonsubstrate peptide, Ac-Asn-Pro-Thr-NH2, was found to adopt the "Asx-turn" in both the solid state and in solution(DMSO-d(6)). The collective data suggest that the ability to form an Asx-turn in the N-glycosylation consensus sequence (Asn-Xaa-Ser/Thr) may be a necessary but not sufficient condition for substrate binding and catalysis.

  DOI：

  10.1021/jo9802123
• 作为产物：
  描述：

  N-(叔丁氧羰基L)-S-甲基-L-半胱氨酸 在 N-甲基吗啉 、 sodium periodate 、 1-羟基苯并三唑 、 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， 反应 1.08h， 生成 tert-butyl N-[(2R)-1-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methylsulfinyl-1-oxopropan-2-yl]carbamate
  参考文献：
  名称：

  Synthesis and Evaluation of Tripeptides Containing Asparagine Analogues as Potential Substrates or Inhibitors of Oligosaccharyltransferase

  摘要：

  The amino acids 5-diazo-4-oxo-L-norvaline, 4-oxo-L-norvaline, and (methanesulfinyl)-L-alanine have been incorporated into three separate tripeptides wherein these nonnatural amino acids replace Asn in a known tripeptide substrate of oligosaccharyltransferase. Synthesis of both the diazoketone- and sulfoxide-containing peptides involved functionalization of the appropriate side chain after peptide assembly, whereas synthesis of the methyl ketone-containing peptide was effected by synthesis of the protected amino acid followed by its incorporation into the desired tripeptide. None of the three synthetic tripeptides showed activity as substrates, nor were they potent inhibitors of oligosaccharyltransferase at concentrations that were 10-35 times the K-m for the corresponding Asn-containing tripeptide substrate. NMR analysis in DMSO-d(6) showed that the diazoketone and methyl ketone peptides adopt the "Asx-turn" conformation, which has been postulated to be crucial for substrate binding. Furthermore, a nonsubstrate peptide, Ac-Asn-Pro-Thr-NH2, was found to adopt the "Asx-turn" in both the solid state and in solution(DMSO-d(6)). The collective data suggest that the ability to form an Asx-turn in the N-glycosylation consensus sequence (Asn-Xaa-Ser/Thr) may be a necessary but not sufficient condition for substrate binding and catalysis.

  DOI：

  10.1021/jo9802123

文献信息

• Synthesis and Evaluation of Tripeptides Containing Asparagine Analogues as Potential Substrates or Inhibitors of Oligosaccharyltransferase
  作者：Tong Xu、R. Marshall Werner、Kwun-Chi Lee、James C. Fettinger、Jeffery T. Davis、James K. Coward

  DOI：10.1021/jo9802123

  日期：1998.7.1

  The amino acids 5-diazo-4-oxo-L-norvaline, 4-oxo-L-norvaline, and (methanesulfinyl)-L-alanine have been incorporated into three separate tripeptides wherein these nonnatural amino acids replace Asn in a known tripeptide substrate of oligosaccharyltransferase. Synthesis of both the diazoketone- and sulfoxide-containing peptides involved functionalization of the appropriate side chain after peptide assembly, whereas synthesis of the methyl ketone-containing peptide was effected by synthesis of the protected amino acid followed by its incorporation into the desired tripeptide. None of the three synthetic tripeptides showed activity as substrates, nor were they potent inhibitors of oligosaccharyltransferase at concentrations that were 10-35 times the K-m for the corresponding Asn-containing tripeptide substrate. NMR analysis in DMSO-d(6) showed that the diazoketone and methyl ketone peptides adopt the "Asx-turn" conformation, which has been postulated to be crucial for substrate binding. Furthermore, a nonsubstrate peptide, Ac-Asn-Pro-Thr-NH2, was found to adopt the "Asx-turn" in both the solid state and in solution(DMSO-d(6)). The collective data suggest that the ability to form an Asx-turn in the N-glycosylation consensus sequence (Asn-Xaa-Ser/Thr) may be a necessary but not sufficient condition for substrate binding and catalysis.