Cysteine sulfinic acid | 35554-99-5

• 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: Cysteine sulfinic acid
• 英文别名: D-Cysteinesulfinic acid；3-sulfino-D-alanine；3-Sulfino-D-alanin；(S)-2-Amino-3-sulfino-propionsaeure；(2S)-2-azaniumyl-3-sulfinopropanoate
• CAS: 35554-99-5
• 化学式: C₃H₇NO₄S
• 分子量: 153.159
• InChiKey: ADVPTQAUNPRNPO-UWTATZPHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  9
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  120
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  D-cysteine 在 cysteine dioxygenase 、 sodium chloride 作用下， 以 aq. phosphate buffer 、 重水 为溶剂， 反应 0.03h， 生成 Cysteine sulfinic acid
  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

• Cavallini et al., Journal of Biological Chemistry, 1958, vol. 230, p. 25,27
  作者：Cavallini et al.

  DOI：——

  日期：——
• Steady-state substrate specificity and O2-coupling efficiency of mouse cysteine dioxygenase
  作者：Wei Li、Brad S. Pierce

  DOI：10.1016/j.abb.2014.11.004

  日期：2015.1

  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.