((1R,2R)-2-hydroxy-1-hydroxymethyl-butyl)-carbamic acid 9H-fluoren-9-ylmethyl ester | 930783-49-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: ((1R,2R)-2-hydroxy-1-hydroxymethyl-butyl)-carbamic acid 9H-fluoren-9-ylmethyl ester
• CAS: 930783-49-6
• 化学式: C₂₀H₂₃NO₄
• 分子量: 341.407
• InChiKey: AMPJKLDEONTLJG-RTBURBONSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.66
• 重原子数：
  25.0
• 可旋转键数：
  6.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  78.79
• 氢给体数：
  3.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  ((1R,2R)-2-hydroxy-1-hydroxymethyl-butyl)-carbamic acid 9H-fluoren-9-ylmethyl ester 在 吡啶 、 硫酸 作用下， 以 二氯甲烷 为溶剂， 反应 64.0h， 生成 ((1R,2R)-2-tert-butoxy-1-hydroxymethyl-butyl)-carbamic acid 9H-fluoren-9-ylmethyl ester
  参考文献：
  名称：

  On the Substrate Specificity of Dehydration by Lacticin 481 Synthetase

  摘要：

  Dehydroamino acids are valuable building blocks that are a challenge to incorporate synthetically into unprotected peptides. Lantibiotic synthetases possess dehydration activity that converts Ser and Thr residues in their peptide substrates into dehydroalanine and dehydrobutyrine residues, respectively. We show here that lacticin 481 synthetase can convert the Thr analogues (R)-3-EtSer, (R)-3-vinylSer, (R)-3-ethynylSer, (R)-3-[(E)-propenyl]Ser, and (R)-3-propynylSer into the corresponding dehydroamino acids when incorporated into its peptide substrate. This relaxed substrate specificity holds promise for using the enzyme for synthetic purposes and for lantibiotic engineering. On the other hand, (R)-3-PrSer, (R)-3-iPrSer, and allo-Thr are not substrates for the enzyme.

  DOI：

  10.1021/ja067672v
• 作为产物：
  描述：

  (2R)-2-aminopentane-1,3-diol 、 氯甲酸-9-芴基甲酯 在 碳酸氢钠 作用下， 以 四氢呋喃 、 水 为溶剂， 反应 1.5h， 以2.06 g的产率得到((1R,2R)-2-hydroxy-1-hydroxymethyl-butyl)-carbamic acid 9H-fluoren-9-ylmethyl ester
  参考文献：
  名称：

  On the Substrate Specificity of Dehydration by Lacticin 481 Synthetase

  摘要：

  Dehydroamino acids are valuable building blocks that are a challenge to incorporate synthetically into unprotected peptides. Lantibiotic synthetases possess dehydration activity that converts Ser and Thr residues in their peptide substrates into dehydroalanine and dehydrobutyrine residues, respectively. We show here that lacticin 481 synthetase can convert the Thr analogues (R)-3-EtSer, (R)-3-vinylSer, (R)-3-ethynylSer, (R)-3-[(E)-propenyl]Ser, and (R)-3-propynylSer into the corresponding dehydroamino acids when incorporated into its peptide substrate. This relaxed substrate specificity holds promise for using the enzyme for synthetic purposes and for lantibiotic engineering. On the other hand, (R)-3-PrSer, (R)-3-iPrSer, and allo-Thr are not substrates for the enzyme.

  DOI：

  10.1021/ja067672v