E. coli Kdo2-Lipid A

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: E. coli Kdo2-Lipid A
• 英文别名: (2R,4R,5R,6R)-2-[(2R,4R,5R,6R)-2-carboxylato-6-[(1R)-1,2-dihydroxyethyl]-2-[[(2R,3S,4R,5R,6R)-5-[[(3R)-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2R,3S,4R,5R,6R)-5-[[(3R)-3-hexadecanoyloxytetradecanoyl]amino]-3-hydroxy-4-[(3R)-3-hydroxytetradecanoyl]oxy-6-phosphonatooxyoxan-2-yl]methoxy]-3-phosphonatooxy-4-[(3R)-3-tetradecanoyloxytetradecanoyl]oxyoxan-2-yl]methoxy]-5-hydroxyoxan-4-yl]oxy-6-[(1R)-1,2-dihydroxyethyl]-4,5-dihydroxyoxane-2-carboxylate
• 化学式: C₁₂₆H₂₂₆N₂O₄₀P₂
• 分子量: 2471.12
• InChiKey: YHHWIOQDRVEIJA-HTCUMWQVSA-H

计算性质

• 辛醇/水分配系数(LogP)：
  31
• 重原子数：
  170
• 可旋转键数：
  110
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.93
• 拓扑面积：
  662
• 氢给体数：
  11
• 氢受体数：
  40

反应信息

• 作为反应物：
  描述：

  E. coli Kdo2-Lipid A 在 肼 作用下， 生成
  参考文献：
  名称：

  Lipopolysaccharide Biosynthesis without the Lipids: Recognition Promiscuity ofEscherichia coliHeptosyltransferase I

  摘要：

  Heptosyltransferase I (HepI) is responsible for the transfer of L-glycero-D-manno-heptose to a 3-deoxy-alpha-D-oct-2-ulopyranosonic acid (Kdo) of the growing core region of lipopolysaccharide (LPS). The catalytic efficiency of HepI with the fully deacylated analogue of Escherichia coli HepI LipidA is 12-fold greater than with the fully acylated substrate, with a k(cat)/K(m) of 2.7 x 10(6) M(-1) s(-1), compared to a value of 2.2 X 10(5) M(-1) s(-1) for the Kdo(2)-LipidA substrate. Not only is this is the first demonstration that an LPS biosynthetic enzyme is catalytically enhanced by the absence of lipids, this result has significant implications for downstream enzymes that are now thought to utilize deacylated substrates.

  DOI：

  10.1021/bi201581b

文献信息

• Lipopolysaccharide Biosynthesis without the Lipids: Recognition Promiscuity of<i>Escherichia coli</i>Heptosyltransferase I
  作者：Daniel J. Czyzyk、Cassie Liu、Erika A. Taylor

  DOI：10.1021/bi201581b

  日期：2011.12.13

  Heptosyltransferase I (HepI) is responsible for the transfer of L-glycero-D-manno-heptose to a 3-deoxy-alpha-D-oct-2-ulopyranosonic acid (Kdo) of the growing core region of lipopolysaccharide (LPS). The catalytic efficiency of HepI with the fully deacylated analogue of Escherichia coli HepI LipidA is 12-fold greater than with the fully acylated substrate, with a k(cat)/K(m) of 2.7 x 10(6) M(-1) s(-1), compared to a value of 2.2 X 10(5) M(-1) s(-1) for the Kdo(2)-LipidA substrate. Not only is this is the first demonstration that an LPS biosynthetic enzyme is catalytically enhanced by the absence of lipids, this result has significant implications for downstream enzymes that are now thought to utilize deacylated substrates.