N-acetyl-1,6-anhydromuramyl-L-Ala-γ-D-Glu-L-Lys | 1222520-56-0

• 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-acetyl-1,6-anhydromuramyl-L-Ala-γ-D-Glu-L-Lys
• 英文别名: (2S)-2-[[(4R)-4-[[(2S)-2-[[(2R)-2-[[(1R,2S,3R,4R,5R)-4-acetamido-2-hydroxy-6,8-dioxabicyclo[3.2.1]octan-3-yl]oxy]propanoyl]amino]propanoyl]amino]-4-carboxybutanoyl]amino]-6-aminohexanoic acid
• CAS: 1222520-56-0
• 化学式: C₂₅H₄₁N₅O₁₂
• 分子量: 603.627
• InChiKey: GWPHFDGMZQKVDT-CPUFMTPVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.4
• 重原子数：
  42
• 可旋转键数：
  17
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  265
• 氢给体数：
  8
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  N-acetyl-1,6-anhydromuramyl-L-Ala-γ-D-Glu-L-Lys 在 periplasmic amidase D 、 zinc(II) chloride 作用下， 生成 1,6-anhydro-N-acetylmuramic acid
  参考文献：
  名称：

  1,6-AnhMurNAc derivatives for assay development of amidase AmiD

  摘要：

  Various peptidoglycan fragments were synthesized from two anhydro-muramic acid derivatives protected with a Bn or a PMB group at the 4th position, in homogenate phase or on a solid support. In order to facilitate HPLC detection, a chromophoric group was attached to the peptide chain. The periplasmic amidase sAmiD of Escherichia coli was used to cleave the amide bond between the lactyl group of the MurNAc and the alpha-amino group of L-Ala where the peptide chain was at least a dipeptide (L-Ala-gamma-D-Glu) amidated by benzylamine on the c-carboxyl group of D-Glu. In the presence of a tripeptide chain (L-Ala-gamma-D-Glu-L-Lys) or a tetrapeptide chain (L-Ala-gamma-D-Glu-m-A(2)pm-D-Ala) higher hydrolysis rates were observed. We have also demonstrated that the presence of TNB on the epsilon-amino group of L-Lys only has a small influence on the hydrolysis capacity of sAmiD. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.09.010
• 作为产物：
  描述：

  在 palladium 10% on activated carbon 、 氢气 作用下， 以 甲醇 为溶剂， 35.0 ℃ 、600.01 kPa 条件下， 反应 72.0h， 以40%的产率得到N-acetyl-1,6-anhydromuramyl-L-Ala-γ-D-Glu-L-Lys
  参考文献：
  名称：

  1,6-AnhMurNAc derivatives for assay development of amidase AmiD

  摘要：

  Various peptidoglycan fragments were synthesized from two anhydro-muramic acid derivatives protected with a Bn or a PMB group at the 4th position, in homogenate phase or on a solid support. In order to facilitate HPLC detection, a chromophoric group was attached to the peptide chain. The periplasmic amidase sAmiD of Escherichia coli was used to cleave the amide bond between the lactyl group of the MurNAc and the alpha-amino group of L-Ala where the peptide chain was at least a dipeptide (L-Ala-gamma-D-Glu) amidated by benzylamine on the c-carboxyl group of D-Glu. In the presence of a tripeptide chain (L-Ala-gamma-D-Glu-L-Lys) or a tetrapeptide chain (L-Ala-gamma-D-Glu-m-A(2)pm-D-Ala) higher hydrolysis rates were observed. We have also demonstrated that the presence of TNB on the epsilon-amino group of L-Lys only has a small influence on the hydrolysis capacity of sAmiD. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.09.010

文献信息

• 1,6-AnhMurNAc derivatives for assay development of amidase AmiD
  作者：Frédéric Mercier、Astrid Zervosen、Nathalie Teller、Jean-Marie Frère、Raphaël Herman、Anne Pennartz、Bernard Joris、André Luxen

  DOI：10.1016/j.bmc.2010.09.010

  日期：2010.11

  Various peptidoglycan fragments were synthesized from two anhydro-muramic acid derivatives protected with a Bn or a PMB group at the 4th position, in homogenate phase or on a solid support. In order to facilitate HPLC detection, a chromophoric group was attached to the peptide chain. The periplasmic amidase sAmiD of Escherichia coli was used to cleave the amide bond between the lactyl group of the MurNAc and the alpha-amino group of L-Ala where the peptide chain was at least a dipeptide (L-Ala-gamma-D-Glu) amidated by benzylamine on the c-carboxyl group of D-Glu. In the presence of a tripeptide chain (L-Ala-gamma-D-Glu-L-Lys) or a tetrapeptide chain (L-Ala-gamma-D-Glu-m-A(2)pm-D-Ala) higher hydrolysis rates were observed. We have also demonstrated that the presence of TNB on the epsilon-amino group of L-Lys only has a small influence on the hydrolysis capacity of sAmiD. (C) 2010 Elsevier Ltd. All rights reserved.