L-高半胱氨酸亚磺酸 | 2686-70-6

• 物质功能分类: 生物化工 - 氨基酸及其衍生物 - 半胱氨酸类衍生物
• 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: L-高半胱氨酸亚磺酸
• 英文名称: L-Homocysteinesulfinic acid
• 英文别名: homocysteine sulfinic acid；L-homocysteine sulphinic acid；L-Homocysteinsulfinsaeure；(2s)-2-Amino-4-sulfinobutanoic acid
• CAS: 2686-70-6
• 化学式: C₄H₉NO₄S
• 分子量: 167.186
• InChiKey: PDNJLMZEGXHSCU-VKHMYHEASA-N

物化性质

• 熔点：
  >165°C (dec.)
• 沸点：
  486.6±55.0 °C(Predicted)
• 密度：
  1.667±0.06 g/cm3(Predicted)
• 溶解度：
  水（轻微，超声处理）
• 稳定性/保质期：

  遵照规定使用和储存，则不会分解。

计算性质

• 辛醇/水分配系数(LogP)：
  -3.8
• 重原子数：
  10
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  120
• 氢给体数：
  3
• 氢受体数：
  6

安全信息

• 危险品标志：
  Xi
• 安全说明：
  S26,S36
• 危险类别码：
  R36/37/38
• WGK Germany：
  3

反应信息

• 作为反应物：
  描述：

  L-高半胱氨酸亚磺酸 在 镍 作用下， 以 水 为溶剂， 反应 0.5h， 生成 L-2-氨基丁酸
  参考文献：
  名称：

  Ohmori, Shinji; Takahashi, Kazuko; Ikeda, Mikiko, Zeitschrift fur Naturforschung, Teil B: Anorganische Chemie, Organische Chemie, 1981, vol. 36, # 3, p. 370 - 374

  摘要：

  DOI：
• 作为产物：
  描述：

  L-高半胱氨酸 在 cysteine dioxygenase 、 sodium chloride 作用下， 以 aq. phosphate buffer 、 重水 为溶剂， 反应 0.03h， 生成 L-高半胱氨酸亚磺酸
  参考文献：
  名称：

  Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase

  摘要：

  Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygendependent oxidation of L-cysteine (Cys) to produce L-cysteine sulfinic acid (CSA). Sequence alignment of mammalian COO with recently discovered thiol dioxygenase enzymes suggests that the mononuclear iron site within all enzymes in this class share a common 3-His first coordination sphere. This implies a similar mechanistic paradigm among thiol dioxygenase enzymes. Although steady-state studies were first reported for mammalian CDO over 45 years ago, detailed analysis of the specificity for alternative thiol-bearing substrates and their oxidative coupling efficiencies have not been reported for this enzyme. Assuming a similar mechanistic theme among this class of enzymes, characterization of the CDO substrate specificity may provide valuable insight into substrate-active site intermolecular during thiol oxidation. In this work, the substrate-specificity for wild-type Mus musculus CDO was investigated using NMR spectroscopy and LC-MS for a variety of thiol-bearing substrates. Tandem mass spectrometry was used to confirm dioxygenase activity for each non-native substrate investigated. Steady-state MichaelisMenten parameters for sulfinic acid product formation and O-2-consumption were compared to establish the coupling efficiency for each reaction. In light of these results, the minimal substrate requirements for CDO catalysis and O-2-activation are discussed. (C) 2014 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.abb.2014.11.004

文献信息

• Reduction of benzyl sulphonyl (sulphone) intermediates to sulphinic acids. Synthesis of hypotaurine, and of<scp>L</scp>-cysteine and<scp>L</scp>-homocysteine sulphinic acids
  作者：D. B. Hope、C. D. Morgan、M. Wälti

  DOI：10.1039/j39700000270

  日期：——

  Reduction of the benzyl sulphonyl derivatives of cysteamine, L-cysteine, and L-homocysteine in liquid ammonia with metallic sodium gave the corresponding sulphinic acids in yields in the range 80–90%.

  用金属钠还原液态氨中的半胱胺，L-半胱氨酸和L-同型半胱氨酸的苄基磺酰基衍生物，其相应的亚磺酸收率在80-90％范围内。