N-lauroyl-tri-L-alanine | 90288-34-9

• 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: N-lauroyl-tri-L-alanine
• 英文别名: lauroyl-L-alanyl-L-alanyl-L-alanine；N-Dodecanoyl-L-alanyl-L-alanyl-L-alanine；(2S)-2-[[(2S)-2-[[(2S)-2-(dodecanoylamino)propanoyl]amino]propanoyl]amino]propanoic acid
• CAS: 90288-34-9
• 化学式: C₂₁H₃₉N₃O₅
• 分子量: 413.558
• InChiKey: OUGULJHGGABFEV-ULQDDVLXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  29
• 可旋转键数：
  16
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.81
• 拓扑面积：
  125
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  月桂酸 、 丙氨酰丙氨酰丙氨酸 在 Streptomyces mobaraensis NBRC 13819 acylase 作用下， 以 甘油 为溶剂， 反应 48.0h， 生成 N-lauroyl-tri-L-alanine
  参考文献：
  名称：

  A Novel Acylase from Streptomyces mobaraensis that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as N-Acyl-l-amino Acids and N-Acyl-peptides

  摘要：

  A novel enzyme that catalyzes efficient hydrolysis of capsaicin (8-methyl-N-vanillyl-6-nonenamide) was isolated from the culture broth of Streptomyces mobaraensis. The enzyme consisted of two dissimilar subunits with molecular masses of 61 and 19 kDa. The enzyme was activated and stabilized in the presence of Co2+. It showed a pH optimum of about 8 and was stable at temperatures of up to 55 degrees C for 1 h at pH 7.8. The specific activity of the enzyme for the hydrolysis of capsaicin was 10(2)-10(4) times higher than those for the enzymes reported to date. In an aqueous/n-hexane biphasic system, capsaicin analogues such as octanoyl, decanoyl, and lauroyl vanillylamides were synthesized from the corresponding fatty acids and vanillylamine at yields of 50% or greater. In addition, the enzyme catalyzed the deacylation of N-lauroyl-L-amino acids and N-lauroyl-L-dipeptides and the efficient synthesis of N alpha-lauroyl-L-lysine, N epsilon-lauroyl-L-lysine, and various N-lauroyl-peptides in aqueous solution in both the absence and the presence of glycerol.

  DOI：

  10.1021/jf052102k

文献信息

• NOVEL SELF-ASSEMBLED AMINO ACID SUPRAMOLECULAR POLYMER, PREPARATION METHOD THEREFOR, AND APPLICATION THEREOF
  申请人：Suzhou Oulit Biopharm Co., Ltd.

  公开号：EP3805249A1

  公开（公告）日：2021-04-14

  Disclosed are a novel self-assembled amino acid supramolecular polymer, a preparation method therefor, and an application thereof. The self-assembled supramolecular polymer is N-lauroyl-L-alanyl-L-alanine or a salt thereof, and the salt thereof comprises sodium N-lauroyl-L-alanyl-L-alaninate and potassium N-lauroyl-L-alanyl-L-alaninate. The disclosed polymer is more effective at inhibiting bacteria and removing pesticides, and can be widely applied to the daily chemical, agricultural, and pharmaceutical industries. Further disclosed are three methods for preparing the compound. The methods produce products in high yields and are suitable for industrial production.

  本发明公开了一种新型自组装氨基酸超分子聚合物、其制备方法及其应用。自组装超分子聚合物为 N-月桂酰基-L-丙氨酰-L-丙氨酸或其盐，其盐包括 N-月桂酰基-L-丙氨酰-L-丙氨酸钠和 N-月桂酰基-L-丙氨酰-L-丙氨酸钾。本发明公开的聚合物在抑菌和去除农药方面效果更佳，可广泛应用于日化、农业和医药行业。进一步公开了制备该化合物的三种方法。这些方法生产的产品收率高，适合工业化生产。
• US4665053A
  申请人：——

  公开号：US4665053A

  公开（公告）日：1987-05-12
• A Novel Acylase from <i>Streptomyces mobaraensis</i> that Efficiently Catalyzes Hydrolysis/Synthesis of Capsaicins as Well as <i>N</i>-Acyl-<scp>l</scp>-amino Acids and <i>N</i>-Acyl-peptides
  作者：Mayuko Koreishi、Demin Zhang、Hiroyuki Imanaka、Koreyoshi Imamura、Shuji Adachi、Ryuichi Matsuno、Kazuhiro Nakanishi

  DOI：10.1021/jf052102k

  日期：2006.1.1

  A novel enzyme that catalyzes efficient hydrolysis of capsaicin (8-methyl-N-vanillyl-6-nonenamide) was isolated from the culture broth of Streptomyces mobaraensis. The enzyme consisted of two dissimilar subunits with molecular masses of 61 and 19 kDa. The enzyme was activated and stabilized in the presence of Co2+. It showed a pH optimum of about 8 and was stable at temperatures of up to 55 degrees C for 1 h at pH 7.8. The specific activity of the enzyme for the hydrolysis of capsaicin was 10(2)-10(4) times higher than those for the enzymes reported to date. In an aqueous/n-hexane biphasic system, capsaicin analogues such as octanoyl, decanoyl, and lauroyl vanillylamides were synthesized from the corresponding fatty acids and vanillylamine at yields of 50% or greater. In addition, the enzyme catalyzed the deacylation of N-lauroyl-L-amino acids and N-lauroyl-L-dipeptides and the efficient synthesis of N alpha-lauroyl-L-lysine, N epsilon-lauroyl-L-lysine, and various N-lauroyl-peptides in aqueous solution in both the absence and the presence of glycerol.