3-(2-furyl)acryloyl-L-methionine | 90281-76-8

• 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
• 英文名称: 3-(2-furyl)acryloyl-L-methionine
• 英文别名: (2S)-2-[3-(furan-2-yl)prop-2-enoylamino]-4-methylsulfanylbutanoic acid
• CAS: 90281-76-8
• 化学式: C₁₂H₁₅NO₄S
• mdl: MFCD03093412
• 分子量: 269.321
• InChiKey: KHFWWYXHMBWCPB-JTQLQIEISA-N

物化性质

• 沸点：
  546.0±50.0 °C(Predicted)
• 密度：
  1.278±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  18
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.333
• 拓扑面积：
  105
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  3-(2-furyl)acryloyl-L-methionine 在 pig kidney aminoacylase-1 作用下， 生成 L-蛋氨酸
  参考文献：
  名称：

  Increasing the synthesis/hydrolysis ratio of aminoacylase 1 by site-directed mutagenesis

  摘要：

  Aminoacylase-1 from pig kidney (pAcy1) catalyzes the highly stereoselective acylation of amino acids, a useful conversion for the preparation of optically pure N-acyl-L-amino acids. The kinetic of this thermodynamically controlled conversion is determined by maximal velocities for synthesis (V-mS) and hydrolysis (V-mH) of the N-acyl-L-amino acid. To investigate which parameter affects maximal velocities, we focused on the proton acceptor potential of the catalytic base, E146, and studied the influence of the active site architecture on its contribution to the pKa of residue E146. The modeled structure of pAcy1 identified residue D346 as having the strongest impact on the electrostatic features of the catalytic base. Substitutions of D346 generally decreased enzymatic activities but also altered both the pH-dependency of hydrolytic activity and the V-mS/V-mH ratio of pAcy1. A reduced theoretical pKa value and a lowered experimental pH optimum of hydrolytic rates for the D346A mutant were associated with a 9-fold increase in V-mS/V-mH. This supports the importance of electrostatic contributions of D346 to the acid-base properties of E146 and demonstrates for the first time the possibility of engineering the V-mS/V-mH ratio of pAcy1. (C) 2009 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.biochi.2009.09.017