N-Formamidine-L-phenylglycine

• 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: N-Formamidine-L-phenylglycine
• 英文别名: (2S)-2-guanidino-2-phenyl-acetic acid；(2S)-2-(diaminomethylideneamino)-2-phenylacetic acid
• 化学式: C₉H₁₁N₃O₂
• 分子量: 193.205
• InChiKey: HBFDNZUFZYXYNY-ZETCQYMHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  14
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  102
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  NVKDR 、 N-Formamidine-L-phenylglycine 在 C₂₆H₄₂N₈O₈ 作用下， 生成 (S)-2-guanidino-2-phenylacetic acid
  参考文献：
  名称：

  A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin

  摘要：

  Peptide natural product backbones are typically made ribosomally or by NRPS machinery. Exploration of pheganomycin biosynthesis defines a third hybrid model in which a grasp ligase joins an NRPS product with a ribosomally produced peptide. Peptide antibiotics are typically biosynthesized by one of two distinct machineries in a ribosome-dependent or ribosome-independent manner. Pheganomycin (PGM (1)) and related analogs consist of the nonproteinogenic amino acid (S)-2-(3,5-dihydroxy-4-hydroxymethyl)phenyl-2-guanidinoacetic acid (2) and a proteinogenic core peptide, making their origin uncertain. We report the identification of the biosynthetic gene cluster from Streptomyces cirratus responsible for PGM production. Unexpectedly, the cluster contains a gene encoding multiple precursor peptides along with several genes plausibly encoding enzymes for the synthesis of amino acid 2. We identified PGM1, which has an ATP-grasp domain, as potentially capable of linking the precursor peptides with 2, and validate this hypothesis using deletion mutants and in vitro reconstitution. We document PGM1's substrate permissivity, which could be rationalized by a large binding pocket as confirmed via structural and mutagenesis experiments. This is to our knowledge the first example of cooperative peptide synthesis achieved by ribosomes and peptide ligases using a peptide nucleophile.

  DOI：

  10.1038/nchembio.1697
• 作为产物：
  描述：

  L-苯甘氨酸 、 二氧化硫脲 在 sodium hydroxide 作用下， 以82.4%的产率得到N-Formamidine-L-phenylglycine
  参考文献：
  名称：

  Preparation of N-Formamidinylamino Acids from Amino and Formamidinesulfinic Acids

  摘要：

  本文介绍了一种实用的合成方法，利用碱性水溶液中的甲酰胺亚磺酸将氨基酸转化为N-甲酰脒基氨基酸。

  DOI：

  10.1055/s-2000-8201

文献信息

• Preparation of N-Formamidinylamino Acids from Amino and Formamidinesulfinic Acids
  作者：Branko S. Jursic、Donna Neumann、Allen McPherson

  DOI：10.1055/s-2000-8201

  日期：——

  A practical synthetic procedure for the conversion of amino acids into N-formamidinylamino acids using formamidinesulfinic acid in basic water solution is presented.

  本文介绍了一种实用的合成方法，利用碱性水溶液中的甲酰胺亚磺酸将氨基酸转化为N-甲酰脒基氨基酸。
• A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin
  作者：Motoyoshi Noike、Takashi Matsui、Koichi Ooya、Ikuo Sasaki、Shouta Ohtaki、Yoshimitsu Hamano、Chitose Maruyama、Jun Ishikawa、Yasuharu Satoh、Hajime Ito、Hiroyuki Morita、Tohru Dairi

  DOI：10.1038/nchembio.1697

  日期：2015.1

  Peptide natural product backbones are typically made ribosomally or by NRPS machinery. Exploration of pheganomycin biosynthesis defines a third hybrid model in which a grasp ligase joins an NRPS product with a ribosomally produced peptide. Peptide antibiotics are typically biosynthesized by one of two distinct machineries in a ribosome-dependent or ribosome-independent manner. Pheganomycin (PGM (1)) and related analogs consist of the nonproteinogenic amino acid (S)-2-(3,5-dihydroxy-4-hydroxymethyl)phenyl-2-guanidinoacetic acid (2) and a proteinogenic core peptide, making their origin uncertain. We report the identification of the biosynthetic gene cluster from Streptomyces cirratus responsible for PGM production. Unexpectedly, the cluster contains a gene encoding multiple precursor peptides along with several genes plausibly encoding enzymes for the synthesis of amino acid 2. We identified PGM1, which has an ATP-grasp domain, as potentially capable of linking the precursor peptides with 2, and validate this hypothesis using deletion mutants and in vitro reconstitution. We document PGM1's substrate permissivity, which could be rationalized by a large binding pocket as confirmed via structural and mutagenesis experiments. This is to our knowledge the first example of cooperative peptide synthesis achieved by ribosomes and peptide ligases using a peptide nucleophile.