D-cysteic acid monohydrate | 1333342-52-1

• 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: D-cysteic acid monohydrate
• 英文别名: (S)-2-Amino-3-sulfopropanoic acid hydrate；(2S)-2-amino-3-sulfopropanoic acid;hydrate
• CAS: 1333342-52-1
• 化学式: C₃H₇NO₅S*H₂O
• 分子量: 187.174
• InChiKey: PCPIXZZGBZWHJO-HSHFZTNMSA-N

反应信息

• 作为产物：
  描述：

  D-胱氨酸 在 盐酸 、 溴 作用下， 以 水 为溶剂， 反应 0.67h， 以34%的产率得到D-cysteic acid monohydrate
  参考文献：
  名称：

  Substrate Specificity of the Aspartate:Alanine Antiporter (AspT) of Tetragenococcus halophilus in Reconstituted Liposomes

  摘要：

  The aspartate: alanine antiporter (AspT) of the lactic acid bacterium Tetragenococcus halophilus is a member of the aspartate: alanine exchanger (AAEx) transporter family. T. halophilus AspT catalyzes the electrogenic exchange of L-aspartate(1-) with L-alanine(0). Although physiological functions of AspT were well studied, L-aspartate(1-) : L-alanine(0) antiport mechanisms are still unsolved. Here we report that the binding sites of L-aspartate and L-alanine are independently present in AspT by means of the kinetic studies. We purified His(6)-tagged T. halophilus AspT and characterized its kinetic properties when reconstituted in liposomes (K-m = 0.35 +/- 0.03 mM for L-aspartate, K-m = 0.098 +/- 0 mM for D-aspartate, K-m = 26 +/- 2 mM for L-alanine, K-m = 3.3 +/- 0.2 mM for D-alanine). Competitive inhibition by various amino acids of L-aspartate or L-alanine in self-exchange reactions revealed that L-cysteine selectively inhibited L-aspartate self-exchange but only weakly inhibited L-alanine self-exchange. Additionally, L-serine selectively inhibited L-alanine self-exchange but barely inhibited L-aspartate self-exchange. The aspartate analogs L-cysteine sulfinic acid, L-cysteic acid, and D-cysteic acid competitively and strongly inhibited L-aspartate self-exchange compared with L-alanine self-exchange. Taken together, these kinetic data suggest that the putative binding sites of L-aspartate and L-alanine are independently located in the substrate translocation pathway of AspT.

  DOI：

  10.1074/jbc.m111.260224