N-磷酰脒基牛磺酸 | 4189-99-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 中文名称: N-磷酰脒基牛磺酸
• 中文别名: 1,1'-[1,1'-联苯基]-4,4'-二基二[2-溴乙烷-1-酮]
• 英文名称: 2-(N'-phosphono-guanidino)-ethanesulfonic acid
• 英文别名: 2-(N'-Phosphono-guanidino)-aethansulfonsaeure；N-Phosphonocarbamimidoyl-taurin；Taurocyanin-phosphat；2-[(Z)-[amino-(phosphonoamino)methylidene]amino]ethanesulfonic acid
• CAS: 4189-99-5
• 化学式: C₃H₁₀N₃O₆PS
• 分子量: 247.169
• InChiKey: JOYGYOHHMWVUFM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.7
• 重原子数：
  14
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  171
• 氢给体数：
  5
• 氢受体数：
  7

安全信息

• 海关编码：
  2931900090

反应信息

• 作为产物：
  描述：

  脒基牛磺酸 在 sodium hydroxide 、 三氯氧磷 作用下， 生成 N-磷酰脒基牛磺酸
  参考文献：
  名称：

  Morrison et al., Biochemical Journal, 1958, vol. 68, p. 447,448,449

  摘要：

  DOI：

文献信息

• Morrison et al., Biochemical Journal, 1958, vol. 68, p. 447,448,449
  作者：Morrison et al.

  DOI：——

  日期：——
• Identification of amino acid residues responsible for taurocyamine binding in mitochondrial taurocyamine kinase from Arenicola brasiliensis
  作者：Kumiko Tanaka、Tamotsu Matsumoto、Tomohiko Suzuki

  DOI：10.1016/j.bbapap.2011.06.003

  日期：2011.10

  In order to investigate the residues associated with binding of the substrate taurocyamine in Arenicola mitochondrial taurocyamine kinase (TK), we performed Ala-scanning of the amino acid sequence HTKTV at positions 67-71 on the GS loop, and determined apparent K(m) and V(max) (appK(m) and appV(max), respectively) of the mutant forms for the substrates taurocyamine and glycocyamine. The appK(m) values for taurocyamine of the K69A, T70A and V71A mutants were significantly increased as compared with wild-type, suggesting that these residues are associated with taurocyamine binding. Of special interest is a property of V71A mutant: its catalytic efficiency for glycocyamine was twice that for taurocyamine, indicating that the V71A mutant acts like a glycocyamine kinase, rather than a TK. The role of the amino acid residue K95 of Arenicola MiTK was also examined. K95 was replaced with R, H. V. I. A and E. K95R, K95H and K95I have a 3-fold higher affinity for taurocyamine, and activity was largely lost in K95E. On the other hand, the K95Y mutant showed a rather unique feature: namely, an increase in substrate concentration caused a decrease in initial velocity of the reaction (substrate inhibition). This is the first report on the key amino acid residues responsible for taurocyamine binding in mitochondrial TK. (C) 2011 Elsevier B.V. All rights reserved.