[1-(R,S)-amino-3-(methylsulphanyl)propyl]phosphinic acid | 67896-53-1

• 分子结构分类: 有机化合物 - 有机硫化合物 - 硫醚类
• 英文名称: [1-(R,S)-amino-3-(methylsulphanyl)propyl]phosphinic acid
• 英文别名: 1-amino-3-(methylthio)propylphosphinic acid；1-amino-3-methylthiopropylphosphinic acid；(1-amino-3-methylsulfanyl-propyl)-phosphinic acid；(1-amino-3-methylsulfanyl-propyl)-phosphonous acid；(1-amino-3-methylsulfanylpropyl)phosphinic acid
• CAS: 67896-53-1；95691-25-1；95691-28-4；65576-99-0
• 化学式: C₄H₁₂NO₂PS
• 分子量: 169.185
• InChiKey: CZRBNMUARBZMHQ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.2
• 重原子数：
  9
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  88.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  [1-(R,S)-amino-3-(methylsulphanyl)propyl]phosphinic acid 在 双氧水 作用下， 以 水 、 溶剂黄146 为溶剂， 反应 0.42h， 以82%的产率得到1-amino-3-(methylsulfinyl)propylphosphinic acid
  参考文献：
  名称：

  含硫氨基酸次膦酸类似物的合成

  摘要：

  合成了蛋氨酸代谢的关键化合物的膦类似物。所得化合物在次膦基或含硫片段处被选择性氧化。

  DOI：

  10.1007/bf02495302
• 作为产物：
  描述：

  3-(methylthio)propanal oxime 在 亚膦酸 作用下， 以 甲醇 为溶剂， 反应 4.0h， 以34.6%的产率得到[1-(R,S)-amino-3-(methylsulphanyl)propyl]phosphinic acid
  参考文献：
  名称：

  含硫氨基酸次膦酸类似物的合成

  摘要：

  合成了蛋氨酸代谢的关键化合物的膦类似物。所得化合物在次膦基或含硫片段处被选择性氧化。

  DOI：

  10.1007/bf02495302

文献信息

• The development of a new class of inhibitors for betaine-homocysteine S-methyltransferase
  作者：Jan Pícha、Václav Vaněk、Miloš Buděšínský、Jana Mládková、Timothy A. Garrow、Jiří Jiráček

  DOI：10.1016/j.ejmech.2013.04.039

  日期：2013.7

  Betaine-homocysteine S-methyltransferase (BHMT) is an important zinc-dependent methyltransferase that uses betaine as the methyl donor for the remethylation of homocysteine to form methionine. In the liver, BHMT performs to half of the homocysteine remethylation. In this study, we systematically investigated the tolerance of the enzyme for modifications at the "homocysteine" part of the previously reported potent inhibitor (R,S)-5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid (1). In the new compounds, which are S-alkylated homocysteine derivatives, we replaced the carboxylic group in the "homocysteine" part of inhibitor 1 with different isosteric moieties (tetrazole and oxadiazolone); we suppressed the carboxylic negative charge by amidations; we enhanced acidity by replacing the carboxylate with phosphonic or phosphinic acids; and we introduced pyrrolidine steric constraints. Some of these compounds display high affinity toward human BHMT and may be useful for further pharmacological studies of this enzyme. Although none of the new compounds were more potent inhibitors than the reference inhibitor 1, this study helped to completely define the structural requirements of the active site of BHMT and revealed the remarkable selectivity of the enzyme for homocysteine. (C) 2013 Elsevier Masson SAS. All rights reserved.
• Baylis, E. Keith; Campbell, Colin D.; Dingwall, John G., Journal of the Chemical Society. Perkin transactions I, 1984, p. 2845 - 2853
  作者：Baylis, E. Keith、Campbell, Colin D.、Dingwall, John G.

  DOI：——

  日期：——
• Stable organophosphorus analogues of S-adenosylmethionine and S-methylmethionine
  作者：Kirill V. Alferov、Yurii N. Zhukov、Elena N. Khurs、Radii M. Khomutov

  DOI：10.1070/mc2003v013n06abeh001856

  日期：2003.1

  The organophosphorus analogues of the biologically significant sulfonium compounds S-adenosylmethionine and S-methylmethionine are much more stable than their carboxylic prototypes.
• DE2722162
  申请人：——

  公开号：——

  公开（公告）日：——
• Synthesis of methionine- and norleucine-derived phosphinopeptides
  作者：Radek Liboska、Jan Pícha、Ivona Hančlová、Miloš Buděšínský、Miloslav Šanda、Jiří Jiráček

  DOI：10.1016/j.tetlet.2008.07.062

  日期：2008.9

  We present herein a straightforward synthesis of N-Fmoc-protected synthons derived from a phosphinic analogue of methionine. These precursors were used Successfully for the solid-phase synthesis of methionine-mimic phosphinopeptides using BOP-catalyzed coupling without protection of the phosphoryl moiety. We also prepared a new type of pseudopeptide derived from a phosphinic analogue of norleucine with a -PO(OH)-CH(2)-COOR moiety. (C) 2008 Elsevier Ltd. All rights reserved.