(3S,4R,5S)-3,4,5-trihydroxyoxan-2-one | 123287-36-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: (3S,4R,5S)-3,4,5-trihydroxyoxan-2-one
• CAS: 123287-36-5
• 化学式: C₅H₈O₅
• 分子量: 148.116
• InChiKey: XXBSUZSONOQQGK-NUNKFHFFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2
• 重原子数：
  10
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  87
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  木糖酸-1,4-内酯 在 Burkholderia multivorans ATCC 17616 amidohydrolase J_04915 作用下， 以 aq. buffer 为溶剂， 生成 (3S,4R,5S)-3,4,5-trihydroxyoxan-2-one
  参考文献：
  名称：

  Discovery of an l-Fucono-1,5-lactonase from cog3618 of the Amidohydrolase Superfamily

  摘要：

  A member of the amidohydrolase superfamily, BmulJ_04915 from Burkholderia multivorans, of unknown function was determined to hydrolyze a series of sugar lactones: L-fiicono-1,4-lactone, n-arabino-1,4-lactone, L-xylono-1,4-lactone, D-lyxono-1,4-lactone, and L-galactono-1,4-lactone. The highest activity was shown for L-fucono-1,4-lactone with a k(cat) value of 140 s(-1) and a k(cat)/K-m value of 1.0 x 10(5) M-1 s(-1) at pH 8.3. The enzymatic product of an adjacent L-fucose dehydrogenase, BmulJ_04919, was shown to be L-fucono-1,5-lactone via nuclear magnetic resonance spectroscopy. L-Fucono-1,5-lactone is unstable and rapidly converts nonenzymatically to L-fucono-1,4-lactone. Because of the chemical instability of L-fiicono-1,5-lactone, 4-deoxy-L-fucono-1,5-lactone was enzymatically synthesized from 4-deoxy-L-fucose using L-fucose dehydrogenase. BmulJ-04915 hydrolyzed 4-deoxy-L-fucono-1,5-lactone with a k(cat) value of 990 s(-1) and a k(cat)/K-m value of 8.0 x 106 M-1 s(-1) at pH 7.1. The protein does not require divalent cations in the active site for catalytic activity. BmulJ_04915 is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a divalent metal for catalytic activity. BmulJ_04915 is the first enzyme that has been shown to catalyze the hydrolysis of either L-fucono-1,4-lactone or L-fucono-1,5-lactone. The structures of the fuconolactonase and the fucose dehydrogenase were determined by X-ray diffraction methods.

  DOI：

  10.1021/bi3015554

文献信息

• Discovery of an <scp>l</scp>-Fucono-1,5-lactonase from cog3618 of the Amidohydrolase Superfamily
  作者：Merlin Eric Hobbs、Matthew Vetting、Howard J. Williams、Tamari Narindoshvili、Devon M. Kebodeaux、Brandan Hillerich、Ronald D. Seidel、Steven C. Almo、Frank M. Raushel

  DOI：10.1021/bi3015554

  日期：2013.1.8

  A member of the amidohydrolase superfamily, BmulJ_04915 from Burkholderia multivorans, of unknown function was determined to hydrolyze a series of sugar lactones: L-fiicono-1,4-lactone, n-arabino-1,4-lactone, L-xylono-1,4-lactone, D-lyxono-1,4-lactone, and L-galactono-1,4-lactone. The highest activity was shown for L-fucono-1,4-lactone with a k(cat) value of 140 s(-1) and a k(cat)/K-m value of 1.0 x 10(5) M-1 s(-1) at pH 8.3. The enzymatic product of an adjacent L-fucose dehydrogenase, BmulJ_04919, was shown to be L-fucono-1,5-lactone via nuclear magnetic resonance spectroscopy. L-Fucono-1,5-lactone is unstable and rapidly converts nonenzymatically to L-fucono-1,4-lactone. Because of the chemical instability of L-fiicono-1,5-lactone, 4-deoxy-L-fucono-1,5-lactone was enzymatically synthesized from 4-deoxy-L-fucose using L-fucose dehydrogenase. BmulJ-04915 hydrolyzed 4-deoxy-L-fucono-1,5-lactone with a k(cat) value of 990 s(-1) and a k(cat)/K-m value of 8.0 x 106 M-1 s(-1) at pH 7.1. The protein does not require divalent cations in the active site for catalytic activity. BmulJ_04915 is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a divalent metal for catalytic activity. BmulJ_04915 is the first enzyme that has been shown to catalyze the hydrolysis of either L-fucono-1,4-lactone or L-fucono-1,5-lactone. The structures of the fuconolactonase and the fucose dehydrogenase were determined by X-ray diffraction methods.