trans,trans-farnesyl-D-cysteine | 141270-80-6

• 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: trans,trans-farnesyl-D-cysteine
• 英文别名: (2S)-2-amino-3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl]sulfanylpropanoic acid
• CAS: 141270-80-6
• 化学式: C₁₈H₃₁NO₂S
• 分子量: 325.516
• InChiKey: SYSLNQMKLROGCL-UINNIIOQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  22
• 可旋转键数：
  11
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.61
• 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：

  trans,trans-farnesyl-D-cysteine 在 sodium hydroxide 、 1-羟基苯并三唑一水物 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 N-acetyl-S-farnesyl-D-cysteine-(D)-α-phenylglycinolamide
  参考文献：
  名称：

  Structure-activity studies on the retinal rod outer segment isoprenylated protein methyltransferase

  摘要：

  Structure-activity studies were performed on the retinal rod outer segment isoprenylated protein methyltransferase that transfers a methyl group from S-adenosylmethionine (AdoMet) to the carboxyl group of isoprenylated (farnesylated or geranylgeranylated) cysteine residues. This methyltransferase enzyme has been shown to methylate N-acetyl-S-farnesyl-L-cysteine (L-AFC, 1) and S-(farnesyl-3-thio)propionic acid (FTP, 2). It is shown here that the enzyme does not enzymatically process D-AFC (8), although D-AFC (8) is a mixed-type inhibitor of the enzyme. Small modifications in the FTP (2) structural series generally lead to inactive substrates. For example, neither the cis- nor the trans-acrylate derivatives of FTP (2) are substrates of the enzyme, but both are inhibitors of it. Alkyl substitutions at the 3-position of FTP (2), moreover, lead to inhibitors of the methyltransferase. Substituents at the 2-position of FTP (2), as in 2-methyl-S-(farnesyl-3-thio)propionic acid (MFTP, 28) or S-farnesyl-2-(thiomethyl)acrylic acid (FTMA, 31), produce active substrates. Modifications at the carboxyl moiety produce neither substrates nor inhibitors of the enzyme. The conclusion from this and earlier studies is that the methyltransferase is selective for an isoprenylated thiopropionate moiety. Small deviations from this minimally essential structure lead to the abolition of substrate activity.

  DOI：

  10.1021/ja00036a052

文献信息

• Structure-activity studies on the retinal rod outer segment isoprenylated protein methyltransferase
  作者：Bryant A. Gilbert、Eng Wui Tan、Dolores Perez-Sala、Robert R. Rando

  DOI：10.1021/ja00036a052

  日期：1992.5

  Structure-activity studies were performed on the retinal rod outer segment isoprenylated protein methyltransferase that transfers a methyl group from S-adenosylmethionine (AdoMet) to the carboxyl group of isoprenylated (farnesylated or geranylgeranylated) cysteine residues. This methyltransferase enzyme has been shown to methylate N-acetyl-S-farnesyl-L-cysteine (L-AFC, 1) and S-(farnesyl-3-thio)propionic acid (FTP, 2). It is shown here that the enzyme does not enzymatically process D-AFC (8), although D-AFC (8) is a mixed-type inhibitor of the enzyme. Small modifications in the FTP (2) structural series generally lead to inactive substrates. For example, neither the cis- nor the trans-acrylate derivatives of FTP (2) are substrates of the enzyme, but both are inhibitors of it. Alkyl substitutions at the 3-position of FTP (2), moreover, lead to inhibitors of the methyltransferase. Substituents at the 2-position of FTP (2), as in 2-methyl-S-(farnesyl-3-thio)propionic acid (MFTP, 28) or S-farnesyl-2-(thiomethyl)acrylic acid (FTMA, 31), produce active substrates. Modifications at the carboxyl moiety produce neither substrates nor inhibitors of the enzyme. The conclusion from this and earlier studies is that the methyltransferase is selective for an isoprenylated thiopropionate moiety. Small deviations from this minimally essential structure lead to the abolition of substrate activity.