1,6-anhydro-N-acetyl-beta-muramate

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 氧杂环己烷
• 英文名称: 1,6-anhydro-N-acetyl-beta-muramate
• 英文别名: (2R)-2-[[(1R,2S,3R,4R,5R)-4-acetamido-2-hydroxy-6,8-dioxabicyclo[3.2.1]octan-3-yl]oxy]propanoate
• 化学式: C11H16NO7-
• 分子量: 274.25
• InChiKey: ZFEGYUMHFZOYIY-YVNCZSHWSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  117
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  1,6-anhydro-N-acetyl-beta-muramate 、 adenosine 5'-triphosphate 、 水 生成 adenosine 5'-diphosphate 、 氢(+1)阳离子 、 N-acetylmuramate 6-phosphate
  参考文献：
  名称：

  Recycling of the Anhydro- N -Acetylmuramic Acid Derived from Cell Wall Murein Involves a Two-Step Conversion to N -Acetylglucosamine-Phosphate

  摘要：

  摘要 大肠杆菌 大肠杆菌能分解其侧壁 60% 以上的木脂素，并将其中的氨基酸成分重新用于合成下一代细胞壁的约 25%。木脂素中的氨基糖也被有效地回收利用。在这里，我们展示了 1,6-anhydro- N -乙酰木氨酸（anhMurNAc）通过转化为 N -乙酰葡糖胺磷酸盐（GlcNAc-P）返回生物合成途径。这种糖首先通过 a nhydro- N -乙酰基 m 尿氨酸 k 酶 (AnmK)的作用，产生 MurNAc-P，随后乙酸酶的作用，裂解了 d -乳酸和 N -乙酰葡糖胺分子之间的键，生成 GlcNAc-P。激酶基因是通过反向遗传学方法确定的。对该酶进行了过表达、纯化和鉴定。细胞提取物 amK 缺失突变体的细胞提取物完全缺乏对 anhMurNAc 的活性。令人惊讶的是，在 anmK 突变体中，anhMurNAc 并未在细胞质中积累，而是出现在培养基中，这表明游离的 anhMurNAc 快速外流。

  DOI：

  10.1128/jb.187.11.3643-3649.2005

文献信息

• MurQ Etherase Is Required by <i>Escherichia coli</i> in Order To Metabolize Anhydro- <i>N</i> -Acetylmuramic Acid Obtained either from the Environment or from Its Own Cell Wall
  作者：Tsuyoshi Uehara、Kyoko Suefuji、Tina Jaeger、Christoph Mayer、James T. Park

  DOI：10.1128/jb.188.4.1660-1662.2006

  日期：2006.2.15

  MurQ is an N -acetylmuramic acid-phosphate (MurNAc-P) etherase that converts MurNAc-P to N -acetylglucosamine-phosphate and is essential for growth on MurNAc as the sole source of carbon (T. Jaegar, M. Arsic, and C. Mayer, J. Biol. Chem. 280: 30100-30106, 2005). Here we show that MurQ is the only MurNAc-P etherase in Escherichia coli and that MurQ and AnmK kinase are required for utilization of anhydro-MurNAc derived either from cell wall murein or imported from the medium.

  摘要 MurQ 是一种 N -乙酰胞壁酸磷酸（MurNAc-P）乙酯酶，可将 MurNAc-P 转化为 N -乙酰葡糖胺磷酸盐，是以 MurNAc 为唯一碳源的生长所必需的（T. Jaegar、M. Arsic 和 C. Mayer，J. Biol.Chem. 280: 30100-30106, 2005).在这里，我们发现 MurQ 是大肠杆菌中唯一的 MurNAc-P 乙酶。 大肠杆菌 而且 MurQ 和 AnmK 激酶是利用从细胞壁金黄色葡萄蛋白或从培养基中导入的脱水-MurNAc 所必需的。
• Molecular Basis of 1,6-Anhydro Bond Cleavage and Phosphoryl Transfer by Pseudomonas aeruginosa 1,6-Anhydro-N-acetylmuramic Acid Kinase
  作者：John-Paul Bacik、Garrett E. Whitworth、Keith A. Stubbs、Anuj K. Yadav、Dylan R. Martin、Ben A. Bailey-Elkin、David J. Vocadlo、Brian L. Mark

  DOI：10.1074/jbc.m110.198317

  日期：2011.4

  Anhydro-N-acetylmuramic acid kinase (AnmK) catalyzes the ATP-dependent conversion of the Gram-negative peptidoglycan (PG) recycling intermediate 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) to N-acetylmuramic acid-6-phosphate (MurNAc-6-P). Here we present crystal structures of Pseudomonas aeruginosa AnmK in complex with its natural substrate, anhMurNAc, and a product of the reaction, ADP. AnmK is homodimeric, with each subunit comprised of two subdomains that are separated by a deep active site cleft, which bears similarity to the ATPase core of proteins belonging to the hexokinase-hsp70-actin superfamily of proteins. The conversion of anhMurNAc to MurNAc-6-P involves both cleavage of the 1,6-anhydro ring of anhMurNAc along with addition of a phosphoryl group to O6 of the sugar, and thus represents an unusual enzymatic mechanism involving the formal addition of H3PO4 to anhMurNAc. The structural complexes and NMR analysis of the reaction suggest that a water molecule, activated by Asp-182, attacks the anomeric carbon of anhMurNAc, aiding cleavage of the 1,6-anhydro bond and facilitating the capture of the gamma phosphate of ATP by O6 via an in-line phosphoryl transfer. AnmK is active only against anhMurNAc and not the metabolically related 1,6-anhydro-N-acetylmuramyl peptides, suggesting that the cytosolic N-acetyl-anhydromuramyl-L-alanine amidase AmpD must first remove the stem peptide from these PG muropeptide catabolites before anhMurNAc can be acted upon by AnmK. Our studies provide the foundation for a mechanistic model for the dual activities of AnmK as a hydrolase and a kinase of an unusual heterocyclic monosaccharide.