Cbz-Thr(α-Man)-Val-OMe | 149834-30-0

• 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: Cbz-Thr(α-Man)-Val-OMe
• 英文别名: methyl (2S)-3-methyl-2-[[(2S,3R)-2-(phenylmethoxycarbonylamino)-3-[(2S,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxybutanoyl]amino]butanoate
• CAS: 149834-30-0
• 化学式: C₂₄H₃₆N₂O₁₁
• 分子量: 528.557
• InChiKey: JIMRUNCOFRWNPM-MHKWPUGKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  37
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  193
• 氢给体数：
  6
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  Cbz-Thr(α-Man)-Val-OMe 在 palladium on activated charcoal 氢气 、 三氟乙酸 作用下， 以 甲醇 为溶剂， 以87%的产率得到Thr(α-Man)-Val-OMe
  参考文献：
  名称：

  Enzymes in oligosaccharide synthesis: active-domain overproduction, specificity study, and synthetic use of an .alpha.-1,2-mannosyltransferase with regeneration of GDP-Man

  摘要：

  The catalytic domain of a membrane-bound alpha-1,2-mannosyltransferase (ManT) from yeast has been overexpressed in E. coli, at a level of approximately 0.7-0.8 units per L with a specific activity of about 1 U/mg (based on a-methyl mannoside) after purification. The E. coli strain has been deposited in ATCC (#77379) and will be available to the public. The isolated ManT is stable in 30% methanol or 20% acetone. It accepts mannose, mannobiose, and O-mannosylglycopeptides as acceptors. A multiple enzyme system with in situ regeneration of GDP-mannose suitable for large-scale synthesis of mannosides and mannosyl glycopeptides has been developed.

  DOI：

  10.1021/jo00067a035
• 作为产物：
  描述：

  Cbz-Thr(α-tetraacetyl-Man)-Val-OMe 在 sodium methylate 作用下， 以 甲醇 为溶剂， 反应 1.5h， 以87%的产率得到Cbz-Thr(α-Man)-Val-OMe
  参考文献：
  名称：

  Wong, Chi-Huey; Schuster, Matthias; Wang, Peng, Journal of the American Chemical Society, 1993, vol. 115, # 14, p. 5893 - 5898

  摘要：

  DOI：

文献信息

• Enzymes in oligosaccharide synthesis: active-domain overproduction, specificity study, and synthetic use of an .alpha.-1,2-mannosyltransferase with regeneration of GDP-Man
  作者：Peng Wang、Gwo Jenn Shen、Yi Fong Wang、Yoshitaka Ichikawa、Chi Huey Wong

  DOI：10.1021/jo00067a035

  日期：1993.7

  The catalytic domain of a membrane-bound alpha-1,2-mannosyltransferase (ManT) from yeast has been overexpressed in E. coli, at a level of approximately 0.7-0.8 units per L with a specific activity of about 1 U/mg (based on a-methyl mannoside) after purification. The E. coli strain has been deposited in ATCC (#77379) and will be available to the public. The isolated ManT is stable in 30% methanol or 20% acetone. It accepts mannose, mannobiose, and O-mannosylglycopeptides as acceptors. A multiple enzyme system with in situ regeneration of GDP-mannose suitable for large-scale synthesis of mannosides and mannosyl glycopeptides has been developed.
• Wong, Chi-Huey; Schuster, Matthias; Wang, Peng, Journal of the American Chemical Society, 1993, vol. 115, # 14, p. 5893 - 5898
  作者：Wong, Chi-Huey、Schuster, Matthias、Wang, Peng、Sears, Pamela

  DOI：——

  日期：——