N-decanoyl-l-homoserine | 947381-68-2

• 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: N-decanoyl-l-homoserine
• 英文别名: (2S)-2-(decanoylamino)-4-hydroxybutanoic acid
• CAS: 947381-68-2
• 化学式: C₁₄H₂₇NO₄
• 分子量: 273.373
• InChiKey: SRVJGOTYLHNRPN-LBPRGKRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  19
• 可旋转键数：
  12
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  86.6
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  N-(2-氧代四氢-3-呋喃基)癸烷酰胺 在 N-acylhomoserine lactonase YS-8 from Geobacillus caldoxylosilyticus, thermophilic bacterium from volcanic soil in Indonesia 作用下， 反应 2.0h， 生成 N-decanoyl-l-homoserine
  参考文献：
  名称：

  Isolation and Characterization ofN-Acylhomoserine Lactonase from the Thermophilic Bacterium,Geobacillus caldoxylosilyticusYS-8

  摘要：

  从印度尼西亚火山土壤中分离出的嗜热硅化细菌YS-8能够降解各种长度和酰基侧链取代的N-酰基高丝氨酸内酯（AHL），降解温度范围为30-70℃。纯化的AHL降解酶显示为32 kDa的单条带，其N端氨基酸序列确定为ANVIKARPKLYVMDN，初步表明AHL降解酶是AHL内酯酶。纯化酶的AHL降解活性在pH 7.5和50℃时达到最大，即使在60℃下热处理3小时后仍能保持约50%的活性，表现出与热稳定酶一致的性质。质谱分析表明，AHL降解酶通过水解内酯，作为AHL内酯酶催化N-3-氧代己酰-L-高丝氨酸内酯和N-己酰-L-高丝氨酸内酯的环状内酯开环。

  DOI：

  10.1271/bbb.110322

文献信息

• Ralstonia ahl-acylase gene
  申请人：Zhang Hui Lian

  公开号：US20050155088A1

  公开（公告）日：2005-07-14

  This invention provides a gene, qsbA, which encodes a protein useful for inactivating certain bacterial quorum-sensing signal molecules (N-acyl homoserine lactones) which participate in bacterial virulence and biofilm differentiation pathways. This gene was isolated from Ralstonia sp., strain XJ12B. The invention also provides the QsbA protein, which possesses N-acyl homoserine lactone inactivating activity.

  本发明提供了一种名为 qsbA 的基因，它编码的蛋白质可用于灭活某些参与细菌毒力和生物膜分化途径的细菌法定量感应信号分子（N-酰基均丝氨酸内酯）。该基因是从 Ralstonia sp., strain XJ12B.本发明还提供了具有 N-酰基均丝氨酸内酯灭活活性的 QsbA 蛋白。
• Enzymic Disruption of N-Aroyl-L-homoserine Lactone-Based Quorum Sensing
  作者：Jessica Momb、Dae-Wi Yoon、Walter Fast

  DOI：10.1002/cbic.201000191

  日期：——
• A Phenylalanine Clamp Controls Substrate Specificity in the Quorum-Quenching Metallo-γ-lactonase from <i>Bacillus thuringiensis</i>
  作者：Ce Feng Liu、Dali Liu、Jessica Momb、Pei W. Thomas、Ashley Lajoie、Gregory A. Petsko、Walter Fast、Dagmar Ringe

  DOI：10.1021/bi400050j

  日期：2013.3.5

  Autoinducer inactivator A (AiiA) is a metal-dependent N-acyl homoserine lactone hydrolase that displays broad substrate specificity but shows a preference for substrates with long N-acyl substitutions. Previously, crystal structures of AiiA in complex with the ring-opened product N-hexanoyl-L-homoserine revealed binding interactions near the metal center but did not identify a binding pocket for the N-acyl chains of longer substrates. Here we report the crystal structure of an AiiA mutant, F107W, determined in the presence and absence of N-decanoyl-L-homoserine. F107 is located in a hydrophobic cavity adjacent to the previously identified ligand binding pocket, and the F107W mutation results in the formation of an unexpected interaction with the ring-opened product. Notably, the structure reveals a previously unidentified hydrophobic binding pocket for the substrate's N-acyl chain. Two aromatic residues, F64 and F68, form a hydrophobic clamp, centered around the seventh carbon in the product-bound structure's decanoyl chain, making an interaction that would also be available for longer substrates, but not for shorter substrates. Steady-state kinetics using substrates of various lengths with AiiA bearing mutations at the hydrophobic clamp, including insertion of a redox-sensitive cysteine pair, confirms the importance of this hydrophobic feature for substrate preference. Identifying the specificity determinants of AiiA will aid the development of more selective quorum-quenching enzymes as tools and as potential therapeutics.
• RALSTONIA AHL-ACYLASE GENE
  申请人：Agency for Science, Technology and Research

  公开号：EP1470221A1

  公开（公告）日：2004-10-27
• US7098014B2
  申请人：——

  公开号：US7098014B2

  公开（公告）日：2006-08-29