5-epi-valiolone | 334709-34-1

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 5-epi-valiolone
• 英文别名: (2R,3S,4S,5R)-2,3,4,5-tetrahydroxy-5-(hydroxymethyl)cyclohexan-1-one
• CAS: 334709-34-1
• 化学式: C₇H₁₂O₆
• 分子量: 192.169
• InChiKey: JCZFNXYQGNLHDQ-BNHYGAARSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3
• 重原子数：
  13
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  118
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  (2,3,4,5,7-五羟基-6-氧代庚基)磷酸二氢酯 在 Val A protein 、 Val D protein, 51.8 kDa, His₆-tagged 、 β-烟酰胺腺嘌呤二核苷酸 、 sodium fluoride 、 cobalt(II) chloride 作用下， 反应 2.0h， 生成 5-epi-valiolone
  参考文献：
  名称：

  Alternative Epimerization in C7N-Aminocyclitol Biosynthesis Is Catalyzed by ValD, A Large Protein of the Vicinal Oxygen Chelate Superfamily

  摘要：

  Gene valD, encodes a large vicinal oxygen chelate (VOC) superfamily protein, has been identified in the validamycin biosynthetic gene cluster. Inactivation of valD significantly reduced validamycin A production, which was fully restored with the full-length valD and partially restored with either N-terminal or C-terminal half by complementation. Heterologously expressed ValD catalyzed the epimerization of 2-epi-5-epi-valiolone to 5-epi-valiolone. This metalloenzyme is a homodimer with a metal ion-binding ratio of 0.73 mol/mole protein toward Fe2+, Mn2+, Ni2+, and Zn2+. Individual and combined site-directed mutations of eight putative active site residues revealed that the N-terminal H44/E107 and the C-terminal H315/E366 are more critical for the activity than the internal H130, E183, H229, and E291. Our data have established ValD as one of the largest proteins of the VOC superfamily, catalyzing an alternative epimerization for C7N-aminocyclitol biosynthesis.

  DOI：

  10.1016/j.chembiol.2009.04.006

文献信息

• Alternative Epimerization in C7N-Aminocyclitol Biosynthesis Is Catalyzed by ValD, A Large Protein of the Vicinal Oxygen Chelate Superfamily
  作者：Hui Xu、Yirong Zhang、Jongtae Yang、Taifo Mahmud、Linquan Bai、Zixin Deng

  DOI：10.1016/j.chembiol.2009.04.006

  日期：2009.5

  Gene valD, encodes a large vicinal oxygen chelate (VOC) superfamily protein, has been identified in the validamycin biosynthetic gene cluster. Inactivation of valD significantly reduced validamycin A production, which was fully restored with the full-length valD and partially restored with either N-terminal or C-terminal half by complementation. Heterologously expressed ValD catalyzed the epimerization of 2-epi-5-epi-valiolone to 5-epi-valiolone. This metalloenzyme is a homodimer with a metal ion-binding ratio of 0.73 mol/mole protein toward Fe2+, Mn2+, Ni2+, and Zn2+. Individual and combined site-directed mutations of eight putative active site residues revealed that the N-terminal H44/E107 and the C-terminal H315/E366 are more critical for the activity than the internal H130, E183, H229, and E291. Our data have established ValD as one of the largest proteins of the VOC superfamily, catalyzing an alternative epimerization for C7N-aminocyclitol biosynthesis.