3-<2-(13)C>decynoic acid | 103322-53-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 3-<2-(13)C>decynoic acid
• 英文别名: 3-<2-13C>decynoic acid
• CAS: 103322-53-8
• 化学式: C₁₀H₁₆O₂
• 分子量: 169.225
• InChiKey: KIZIQHLTPZNNRL-QBZHADDCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.43
• 重原子数：
  12.0
• 可旋转键数：
  5.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  37.3
• 氢给体数：
  1.0
• 氢受体数：
  1.0

反应信息

• 作为反应物：
  描述：

  3-<2-(13)C>decynoic acid 在 草酰氯 、 乙醇 、 sodium ethanolate 作用下， 以 吡啶 、 苯 为溶剂， 反应 0.78h， 生成 2,3-<2-(13)C>decadienethioic acid S-1-propyl ester
  参考文献：
  名称：

  .beta.-Hydroxydecanoyl thioester dehydrase. Complete characterization of the fate of the "suicide" substrate 3-decynoyl-NAC

  摘要：

  DOI：

  10.1021/ja00277a041
• 作为产物：
  描述：

  2-<1-(13)C>nonyn-1-ol 在 盐酸 、 sodium hydroxide 、 三溴化磷 、 lithium bromide 作用下， 以 吡啶 、 甲醇 、 乙醚 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 27.67h， 生成 3-<2-(13)C>decynoic acid
  参考文献：
  名称：

  .beta.-Hydroxydecanoyl thioester dehydrase. Complete characterization of the fate of the "suicide" substrate 3-decynoyl-NAC

  摘要：

  DOI：

  10.1021/ja00277a041

文献信息

• Chemistry and Photochemistry Attending the Inactivation of Escherichia coli .beta.-Hydroxydecanoyl Thiol Ester Dehydrase by an Acetylenic Diazoketone
  作者：Barry S. Henderson、Barbara S. Larsen、John M. Schwab

  DOI：10.1021/ja00091a001

  日期：1994.6

  beta-Hydroxydecanoyl thiol ester dehydrase from Escherichia coli, an enzyme that catalyzes both dehydration and allylic rearrangement reactions, has been shown previously to undergo mechanism-based inactivation by the acetylenic substrate analog 1-diazo-4-undecyn-2-one (DUO). Details of the chemistry and photochemistry of DUO are now presented. Analysis of DUO-inactivated dehydrase by N-15 NMR spectroscopy indicates that DUO quantitatively alkylates histidine-70. Long-wavelength photoirradiation leads to spectrophotometrically observable changes in the DUO-dehydrase adduct. The structural changes were characterized by a combination of methods. Samples of protein that had been inactivated with [1-C-13]-, [(2)-C-13]-, and [3-C-13]DUO were analyzed by C-13 NMR spectroscopy, both prior and subsequent to photoirradiation. By comparisons of the chemical shifts of the enriched atoms of the inactivator moiety with those of model compounds, it was confirmed that the alpha-diazoketone moiety is retained in DUO-inactivated dehydrase and that photoirradiation leads to Wolff rearrangement of the alpha-diazoketone moiety followed by attack of a nucleophile on the resulting ketene. Proteolytic degradation of photoirradiated; DUO-inactivated dehydrase gave peptides that were analyzed by Edman sequencing and by mass spectrometry. The results are consistent with a single protein modification (at H70), and attack on the ketene by water, leading to a carboxylic acid. Samples of intact native, DUO-inactivated, and photoirradiated, DUO-inactivated dehydrase were analyzed by electrospray ionization mass spectrometry, the results of which clearly support the hypothesis that the ketene suffers attack by water. In light of recent results from X-ray crystallography, it is proposed that the water that attacks the ketene is one of two bound water molecules with specific roles in the binding and/or catalytic turnover of substrate. A Michael addition-elimination mechanism is presented to explain the unexpected hydrolytic lability of the DUO-dehydrase adduct.