uridine-5'-diphosphate-N-acetylmuramoyl-L-alanine-D-glutamate

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: uridine-5'-diphosphate-N-acetylmuramoyl-L-alanine-D-glutamate
• 英文别名: UDP-MurNAc-L-Ala-D-Glu；(2R)-2-[[(2S)-2-[[(2R)-2-[(2R,3R,4R,5S,6R)-3-acetamido-2-[[[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxypropanoyl]amino]propanoyl]amino]pentanedioic acid
• 化学式: C₂₈H₄₃N₅O₂₃P₂
• 分子量: 879.617
• InChiKey: OJZCATPXPWFLHF-HPUCEMLMSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.3
• 重原子数：
  58.0
• 可旋转键数：
  20.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  427.66
• 氢给体数：
  12.0
• 氢受体数：
  20.0

反应信息

• 作为产物：
  描述：

  UDP-N-acetylmuramic acid α-anomer 在 硫酸氢铵 、 E_. coli MurD 、 enzyme MurC 、 5’-三磷酸腺苷 、 2-巯基乙醇 、 magnesium chloride 作用下， 以 aq. buffer 为溶剂， 反应 16.0h， 生成 uridine-5'-diphosphate-N-acetylmuramoyl-L-alanine-D-glutamate
  参考文献：
  名称：

  A Glycopeptidyl-Glutamate Epimerase for Bacterial Peptidoglycan Biosynthesis

  摘要：

  D-Glutamate (Glu) supplied by Glu racemases or D-amino acid transaminase is utilized for peptidoglycan biosynthesis in microorganisms. Comparative genomics has shown that some microorganisms, including Xanthomonas oryzae, perhaps have no orthologues of these genes. We performed shotgun cloning experiments with a D-Glu auxotrophic Escherichia coli mutant as the host and X. oryzae as the DNA donor. We obtained complementary genes, XOO_1319 and XOO_1320, which are annotated as a hypothetical protein and MurD (UDP-MurNAc-L-Ala-D-Glu synthetase), respectively. By detailed in vitro analysis, we revealed that XOO_1320 is an enzyme to ligate L-Glu to UDP-MurNAc-L-Ala, providing the first example of MurD utilizing L-Glu, and that XOO_1319 is a novel enzyme catalyzing epimerization of the terminal L-Glu of the product in the presence of ATP and Mg2+. We investigated the occurrence of XOO_1319 orthologues and found that it exists in some categories of microorganisms, including pathogenic ones.

  DOI：

  10.1021/jacs.7b01221

文献信息

• A Glycopeptidyl-Glutamate Epimerase for Bacterial Peptidoglycan Biosynthesis
  作者：Ruoyin Feng、Yasuharu Satoh、Yasushi Ogasawara、Tohru Yoshimura、Tohru Dairi

  DOI：10.1021/jacs.7b01221

  日期：2017.3.29

  D-Glutamate (Glu) supplied by Glu racemases or D-amino acid transaminase is utilized for peptidoglycan biosynthesis in microorganisms. Comparative genomics has shown that some microorganisms, including Xanthomonas oryzae, perhaps have no orthologues of these genes. We performed shotgun cloning experiments with a D-Glu auxotrophic Escherichia coli mutant as the host and X. oryzae as the DNA donor. We obtained complementary genes, XOO_1319 and XOO_1320, which are annotated as a hypothetical protein and MurD (UDP-MurNAc-L-Ala-D-Glu synthetase), respectively. By detailed in vitro analysis, we revealed that XOO_1320 is an enzyme to ligate L-Glu to UDP-MurNAc-L-Ala, providing the first example of MurD utilizing L-Glu, and that XOO_1319 is a novel enzyme catalyzing epimerization of the terminal L-Glu of the product in the presence of ATP and Mg2+. We investigated the occurrence of XOO_1319 orthologues and found that it exists in some categories of microorganisms, including pathogenic ones.