GDP-alpha-D-mannuronate

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: GDP-alpha-D-mannuronate
• 英文别名: (2S,3S,4S,5S,6R)-6-[[[(2R,3S,4R,5R)-5-(2-amino-6-oxo-1H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-oxidophosphoryl]oxy-oxidophosphoryl]oxy-3,4,5-trihydroxyoxane-2-carboxylate
• 化学式: C16H20N5O17P2-3
• 分子量: 616.3
• InChiKey: DNBSDUDYNPJVCN-ZXTXFPBHSA-K

计算性质

• 辛醇/水分配系数(LogP)：
  -6.3
• 重原子数：
  40
• 可旋转键数：
  8
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  353
• 氢给体数：
  7
• 氢受体数：
  18

反应信息

• 作为产物：
  描述：

  guanosine 5'-diphospho-1-α-D-mannose 、 水 、 nicotinamide adenine dinucleotide 生成 GDP-alpha-D-mannuronate 、 氢(+1)阳离子 、 NADH
  参考文献：
  名称：

  Crystal Structure of GDP-Mannose Dehydrogenase:  A Key Enzyme of Alginate Biosynthesis in P. aeruginosa^,

  摘要：

  The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in the synthesis of the exopolysaccharide alginate. Alginate is a major component of P. aeruginosa biofilms that protect the bacteria from the host immune response and antibiotic therapy. The 1.55 Angstrom crystal structure of GMD in ternary complex with its cofactor NAD(H) and product GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer with two polypeptide chains contributing to each active site. The extensive dimer interface provides multiple opportunities for intersubunit communication. Comparison of the GMD structure with that of UDP-glucose dehydrogenase reveals the structural basis of sugar binding specificity that distinguishes these two related enzyme families. The high-resolution structure of GMD provides detailed information on the active site of the enzyme and a template for structure-based inhibitor design.

  DOI：

  10.1021/bi027328k

文献信息

• Roychoudhury S.; May T.B.; Gill J.F., J Biol Chem, 1989, 0021-9258, 9380-5
  作者：Roychoudhury S.、May T.B.、Gill J.F.、Singh S.K.、Feingold D.S.、Chakrabarty A.M.

  DOI：——

  日期：——
• Crystal Structure of GDP-Mannose Dehydrogenase:  A Key Enzyme of Alginate Biosynthesis in <i>P. aeruginosa</i>^,
  作者：Christopher F. Snook、Peter A. Tipton、Lesa J. Beamer

  DOI：10.1021/bi027328k

  日期：2003.4.1

  The enzyme GMD from Pseudomonas aeruginosa catalyzes the committed step in the synthesis of the exopolysaccharide alginate. Alginate is a major component of P. aeruginosa biofilms that protect the bacteria from the host immune response and antibiotic therapy. The 1.55 Angstrom crystal structure of GMD in ternary complex with its cofactor NAD(H) and product GDP-mannuronic acid reveals that the enzyme forms a domain-swapped dimer with two polypeptide chains contributing to each active site. The extensive dimer interface provides multiple opportunities for intersubunit communication. Comparison of the GMD structure with that of UDP-glucose dehydrogenase reveals the structural basis of sugar binding specificity that distinguishes these two related enzyme families. The high-resolution structure of GMD provides detailed information on the active site of the enzyme and a template for structure-based inhibitor design.