(2R,6S)-2-amino-6-[[(4R)-4-[[(2S)-2-aminopropanoyl]amino]-4-carboxybutanoyl]amino]-7-[[(1R)-1-carboxyethyl]amino]-7-oxoheptanoic acid | 23557-98-4

• 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: (2R,6S)-2-amino-6-[[(4R)-4-[[(2S)-2-aminopropanoyl]amino]-4-carboxybutanoyl]amino]-7-[[(1R)-1-carboxyethyl]amino]-7-oxoheptanoic acid
• CAS: 23557-98-4
• 化学式: C₁₈H₃₁N₅O₉
• 分子量: 461.472
• InChiKey: VFGFFQOPKZHQLZ-MTVMDMGHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.2
• 重原子数：
  32
• 可旋转键数：
  15
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  251
• 氢给体数：
  8
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  在 ampDh₃ gene from Pseudomonas aeruginosa 、 溶剂黄146 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 38.5h， 生成 (2R,6S)-2-amino-6-[[(4R)-4-[[(2S)-2-aminopropanoyl]amino]-4-carboxybutanoyl]amino]-7-[[(1R)-1-carboxyethyl]amino]-7-oxoheptanoic acid
  参考文献：
  名称：

  Reactions of the Three AmpD Enzymes of Pseudomonas aeruginosa

  摘要：

  A group of Gram-negative bacteria, including the problematic pathogen Pseudomonas aeruginosa, has linked the steps in cell-wall recycling with the ability to manifest resistance to beta-lactam antibiotics. A key step at the crossroads of the two events is performed by the protease AmpD, which hydrolyzes the peptide in the metabolite that influences these events. In contrast to other organisms that harbor this elaborate system, the genomic sequences of P. aeruginosa reveal it to have three paralogous genes for this protease, designated as ampD, ampDh2, and ampDh3. The recombinant gene products were purified to homogeneity, and their functions were assessed by the use of synthetic samples of three bacterial metabolites in cell-wall recycling and of three surrogates of cell-wall peptidoglycan. The results unequivocally identify AmpD as the bona fide recycling enzyme and AmpDh2 and AmpDh3 as enzymes involved in turnover of the bacterial cell wall itself. These findings define for the first time the events mediated by these three enzymes that lead to turnover of a key cell-wall recycling metabolite as well as the cell wall itself in its maturation.

  DOI：

  10.1021/ja400970n

文献信息

• Development of solid-supported methodology for the preparation of peptidoglycan fragments containing (2S,6R)-diaminopimelic acid
  作者：Justine F. Simon、Nicolas Lamborelle、Astrid Zervosen、Christian Lemaire、Bernard Joris、André Luxen

  DOI：10.1016/j.tetlet.2016.02.098

  日期：2016.4

  consists of a Wang resin anchored by an amino acid chain including allylglycine. By olefin cross metathesis with vinylglycine, unsaturated protected (2S,6R)-A2pm was fixed on solid support. Peptides were achieved by cleavage of cross metathesis products from resin, followed by reduction of double bonds along removing of protecting groups. Furthermore, this efficient solid phase approach will lead to peptide

  在这里，我们描述了一种有效的固体支持方法的开发，该方法用于立体选择性合成两个含有（2 S，6 R）-二氨基庚二酸，（S）-Ala-γ-（R）-Glu-（2 S， 6 R）-A 2 pm-（R）-Ala 1和γ-（R）-Glu-（2 S，6 R）-A 2 pm 2。该平台由Wang树脂组成，该Wang树脂由包含烯丙基甘氨酸的氨基酸链锚定。通过乙烯基甘氨酸与烯烃交叉复分解，得到不饱和保护的（2 S，6 R）-A 2下午固定在坚实的支持。通过从树脂上裂解交叉复分解产物，然后沿着去除保护基团的双键还原来获得肽。此外，这种有效的固相方法将产生肽和多肽文库。
• Reactions of the Three AmpD Enzymes of <i>Pseudomonas aeruginosa</i>
  作者：Weilie Zhang、Mijoon Lee、Dusan Hesek、Elena Lastochkin、Bill Boggess、Shahriar Mobashery

  DOI：10.1021/ja400970n

  日期：2013.4.3

  A group of Gram-negative bacteria, including the problematic pathogen Pseudomonas aeruginosa, has linked the steps in cell-wall recycling with the ability to manifest resistance to beta-lactam antibiotics. A key step at the crossroads of the two events is performed by the protease AmpD, which hydrolyzes the peptide in the metabolite that influences these events. In contrast to other organisms that harbor this elaborate system, the genomic sequences of P. aeruginosa reveal it to have three paralogous genes for this protease, designated as ampD, ampDh2, and ampDh3. The recombinant gene products were purified to homogeneity, and their functions were assessed by the use of synthetic samples of three bacterial metabolites in cell-wall recycling and of three surrogates of cell-wall peptidoglycan. The results unequivocally identify AmpD as the bona fide recycling enzyme and AmpDh2 and AmpDh3 as enzymes involved in turnover of the bacterial cell wall itself. These findings define for the first time the events mediated by these three enzymes that lead to turnover of a key cell-wall recycling metabolite as well as the cell wall itself in its maturation.