[(3S)-3-aminooxolan-2-ylidene]oxidanium

• 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: [(3S)-3-aminooxolan-2-ylidene]oxidanium
• 化学式: C4H8NO2+
• 分子量: 102.11
• InChiKey: QJPWUUJVYOJNMH-VKHMYHEASA-O

计算性质

• 辛醇/水分配系数(LogP)：
  -0.6
• 重原子数：
  7
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  53.9
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  an N-acyl-L-homoserine lactone 、 水 生成 a carboxylate 、 [(3S)-3-aminooxolan-2-ylidene]oxidanium
  参考文献：
  名称：

  铜绿假单胞菌PAO1的N-酰基高丝氨酸内酯酰基转移酶猝灭群体。

  摘要：

  机会性人类病原体铜绿假单胞菌PAO1的毒力由N-酰基高丝氨酸内酯（AHL）依赖性群体感应系统控制。在铜绿假单胞菌PAO1基因组中假定的酰基转移酶基因的功能分析过程中，发现PA2385基因编码一种酰基转移酶，可从依赖AHL的群体感应信号分子的高丝氨酸内酯（HSL）核中去除脂肪酸侧链。分析表明，酰基转移酶的翻译后加工过程和水解反应类型与β-内酰胺酰化酶相似，强烈表明PA2385蛋白是N末端亲核水解酶超家族的成员。在生物测定中，在生理学上相关的低浓度下，纯化的酰基转移酶可降解具有11至14个碳原子长度的侧链的AHL降解。在侧链的3'位置的取代基不影响活性，表明宽范围的AHL群体猝灭活性。在铜绿假单胞菌PAO1的两个主要AHL信号分子中，仅N-丁酰基-1-高丝氨酸内酯（C4-HSL）和N-（3-氧十二烷酰基）-1-高丝氨酸内酯（3-oxo-C12-HSL）该酶降解了3-氧代-C12-HSL。将纯化

  DOI：

  10.1128/iai.74.3.1673-1682.2006

文献信息

• A probable aculeacin A acylase from the Ralstonia solanacearum GMI1000 is N-acyl-homoserine lactone acylase with quorum-quenching activity
  作者：Chin-Nung Chen、Chii-Jaan Chen、Chen-Ting Liao、Chia-Yin Lee

  DOI：10.1186/1471-2180-9-89

  日期：2009.12

  RESULTS An aac gene of undemonstrated function from Ralstonia solanacearum GMI1000 was cloned, expressed in Escherichia coli; it inactivated four AHLs that were tested. The sequence of the 795 amino acid polypeptide was considerably similar to the AHL-acylase from Ralstonia sp. XJ12B with 83% identity match and shared 39% identity with an aculeacin A acylase precursor from the gram-positive actinomycete

  背景技术具有群体感应系统的多种植物和动物病原体的感染和毒力功能受作为信号分子的 N-酰基高丝氨酸内酯 (AHL) 的调节。AHL-酰化酶是一种群体淬灭酶，通过从 AHL 的高丝氨酸内酯环上去除脂肪酸侧链来降解 AHL。这阻止了群体感应细菌中的 AHL 积累和致病表型。结果从青枯病菌GMI1000中克隆到一个功能未明的aac基因，在大肠杆菌中表达；它灭活了四个经过测试的 AHL。795 个氨基酸多肽的序列与来自 Ralstonia sp. 的 AHL 酰化酶非常相似。XJ12B 与来自革兰氏阳性放线菌 Actinoplanes utahensis 的 Aculeacin A 酰基转移酶前体具有 83% 的同一性匹配和 39% 的同一性。Aculeacin A 是一种中性脂肽类抗生素和抗真菌药物。电喷雾电离质谱 (ESI-MS) 分析证实 Aac 水解 AHL 的酰胺键，释放高丝氨酸内酯和相应的脂肪酸。然而，ESI-MS
• Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes
  作者：Yi-Han Lin、Jin-Ling Xu、Jiangyong Hu、Lian-Hui Wang、Say Leong Ong、Jared Renton Leadbetter、Lian-Hui Zhang

  DOI：10.1046/j.1365-2958.2003.03351.x

  日期：——

  Summary N ‐acylhomoserine lactones (AHLs) are used as signal molecules by many quorum‐sensing Proteobacteria. Diverse plant and animal pathogens use AHLs to regulate infection and virulence functions. These signals are subject to biological inactivation by AHL‐lactonases and AHL‐acylases. Previously, little was known about the molecular details underlying the latter mechanism. An AHL signal‐inactivating bacterium, identified as a Ralstonia sp., was isolated from a mixed‐species biofilm. The signal inactivation encoding gene from this organism, which we call aiiD , was cloned and successfully expressed in Escherichia coli and inactivated three AHLs tested. The predicted 794‐amino‐acid polypeptide was most similar to the aculeacin A acylase (AAC) from Actinoplanes utahensis and also shared significant similarities with cephalosporin acylases and other N‐terminal (Ntn) hydrolases. However, the most similar homologues of AiiD are deduced proteins of undemonstrated function from available Ralstonia , Deinococcus and Pseudomonas genomes. LC‐MS analyses demonstrated that AiiD hydrolyses the AHL amide, releasing homoserine lactone and the corresponding fatty acid. Expression of AiiD in Pseudomonas aeruginosa PAO1 quenched quorum sensing by this bacterium, decreasing its ability to swarm, produce elastase and pyocyanin and to paralyse nematodes. Thus, AHL‐acylases have fundamental implications and hold biotechnological promise in quenching quorum sensing.