[(3S)-3-乙酰氨基-4-羟基-4-氧代丁基]-羟基-氧代鏻 | 135093-66-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 中文名称: [(3S)-3-乙酰氨基-4-羟基-4-氧代丁基]-羟基-氧代鏻
• 英文名称: N-acetyldemethylphosphinothricin
• 英文别名: (2S)-2-acetamido-4-hydroxyphosphonoylbutanoic acid
• CAS: 135093-66-2
• 化学式: C₆H₁₂NO₅P
• 分子量: 209.139
• InChiKey: VMEBCHDZEJWXIU-YFKPBYRVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.8
• 重原子数：
  13
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  104
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  methylcobalamin 、 [(3S)-3-乙酰氨基-4-羟基-4-氧代丁基]-羟基-氧代鏻 在 titanium(III) citrate 、 cobalamin dependent radical S-adenosyl-L-methionine methyltransferase from Shewanella denitrificans OS₂₁₇ 、 P-methyltransferase from Kitasatospora phosalacinea 作用下， 以 aq. buffer 为溶剂， 反应 18.0h， 生成 L-2-acetamido-4-(hydroxymethylphosphinyl)butanoic acid
  参考文献：
  名称：

  Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217

  摘要：

  Natural products containing carbon-phosphorus bonds elicit important bioactivity in many organisms. L-Phosphinothricin contains the only known naturally-occurring carbon-phosphorus-carbon bond linkage. In actinomycetes, the cobalamin-dependent radical S-adenosyl-L-methionine (SAM) methyltransferase PhpK catalyzes the formation of the second C-P bond to generate the complete C-P-C linkage in phosphinothricin. Here we use electron paramagnetic resonance and nuclear magnetic resonance spectroscopies to characterize and demonstrate the activity of a cobalamin-dependent radical SAM methyltransferase denoted SD_1168 from Shewanella denitrificans OS217, a marine bacterium that has not been reported to synthesize phosphinothricin. Recombinant, refolded, and reconstituted SD_1168 binds a four-iron, four-sulfur cluster that interacts with SAM and cobalamin. In the presence of SAM, a reductant, and methylcobalamin, SD_1168 surprisingly catalyzes the P-methylation of N-acetyl-demethylphosphinothricin and demethylphosphinothricin to produce N-acetyl-phosphinothricin and phosphinothricin, respectively. In addition, this enzyme is active in the absence of methylcobalamin if the strong reductant titanium (III) citrate and hydroxocobalamin are provided. When incubated with [methyl-C-13] cobalamin and titanium citrate, both [methyl-C-13] and unlabeled N-acetylphosphinothricin are produced. Our results suggest that SD_1168 catalyzes P-methylation using radical SAM-dependent chemistry with cobalamin as a coenzyme. In light of recent genomic information, the discovery of this P-methyltransferase suggests that S. denitnficans produces a phosphinate natural product. (C) 2014 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.bbapap.2014.09.009
• 作为产物：
  描述：

  L-2-amino-4-hydroxyphosphinylbutanoic acid 、 乙酸酐 在 溶剂黄146 、 三乙胺 作用下， 反应 24.0h， 生成 [(3S)-3-乙酰氨基-4-羟基-4-氧代丁基]-羟基-氧代鏻
  参考文献：
  名称：

  Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217

  摘要：

  Natural products containing carbon-phosphorus bonds elicit important bioactivity in many organisms. L-Phosphinothricin contains the only known naturally-occurring carbon-phosphorus-carbon bond linkage. In actinomycetes, the cobalamin-dependent radical S-adenosyl-L-methionine (SAM) methyltransferase PhpK catalyzes the formation of the second C-P bond to generate the complete C-P-C linkage in phosphinothricin. Here we use electron paramagnetic resonance and nuclear magnetic resonance spectroscopies to characterize and demonstrate the activity of a cobalamin-dependent radical SAM methyltransferase denoted SD_1168 from Shewanella denitrificans OS217, a marine bacterium that has not been reported to synthesize phosphinothricin. Recombinant, refolded, and reconstituted SD_1168 binds a four-iron, four-sulfur cluster that interacts with SAM and cobalamin. In the presence of SAM, a reductant, and methylcobalamin, SD_1168 surprisingly catalyzes the P-methylation of N-acetyl-demethylphosphinothricin and demethylphosphinothricin to produce N-acetyl-phosphinothricin and phosphinothricin, respectively. In addition, this enzyme is active in the absence of methylcobalamin if the strong reductant titanium (III) citrate and hydroxocobalamin are provided. When incubated with [methyl-C-13] cobalamin and titanium citrate, both [methyl-C-13] and unlabeled N-acetylphosphinothricin are produced. Our results suggest that SD_1168 catalyzes P-methylation using radical SAM-dependent chemistry with cobalamin as a coenzyme. In light of recent genomic information, the discovery of this P-methyltransferase suggests that S. denitnficans produces a phosphinate natural product. (C) 2014 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.bbapap.2014.09.009

文献信息

• Spectroscopic characterization and mechanistic investigation of P-methyl transfer by a radical SAM enzyme from the marine bacterium Shewanella denitrificans OS217
  作者：Kylie D. Allen、Susan C. Wang

  DOI：10.1016/j.bbapap.2014.09.009

  日期：2014.12

  Natural products containing carbon-phosphorus bonds elicit important bioactivity in many organisms. L-Phosphinothricin contains the only known naturally-occurring carbon-phosphorus-carbon bond linkage. In actinomycetes, the cobalamin-dependent radical S-adenosyl-L-methionine (SAM) methyltransferase PhpK catalyzes the formation of the second C-P bond to generate the complete C-P-C linkage in phosphinothricin. Here we use electron paramagnetic resonance and nuclear magnetic resonance spectroscopies to characterize and demonstrate the activity of a cobalamin-dependent radical SAM methyltransferase denoted SD_1168 from Shewanella denitrificans OS217, a marine bacterium that has not been reported to synthesize phosphinothricin. Recombinant, refolded, and reconstituted SD_1168 binds a four-iron, four-sulfur cluster that interacts with SAM and cobalamin. In the presence of SAM, a reductant, and methylcobalamin, SD_1168 surprisingly catalyzes the P-methylation of N-acetyl-demethylphosphinothricin and demethylphosphinothricin to produce N-acetyl-phosphinothricin and phosphinothricin, respectively. In addition, this enzyme is active in the absence of methylcobalamin if the strong reductant titanium (III) citrate and hydroxocobalamin are provided. When incubated with [methyl-C-13] cobalamin and titanium citrate, both [methyl-C-13] and unlabeled N-acetylphosphinothricin are produced. Our results suggest that SD_1168 catalyzes P-methylation using radical SAM-dependent chemistry with cobalamin as a coenzyme. In light of recent genomic information, the discovery of this P-methyltransferase suggests that S. denitnficans produces a phosphinate natural product. (C) 2014 Elsevier B.V. All rights reserved.