YALPETGK | 950832-64-1

• 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: YALPETGK
• 英文别名: H-Tyr-Ala-Leu-Pro-Glu-Thr-Gly-Lys-OH；(2S)-6-amino-2-[[2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]-4-carboxybutanoyl]amino]-3-hydroxybutanoyl]amino]acetyl]amino]hexanoic acid
• CAS: 950832-64-1
• 化学式: C₄₀H₆₃N₉O₁₃
• 分子量: 877.993
• InChiKey: GZFBMZGUUXADMR-UAQCUNDISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6
• 重原子数：
  62
• 可旋转键数：
  26
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  362
• 氢给体数：
  12
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  YALPETGK 在 Staphyloccocus aureus recombinant transpeptidase sortase A 、 2-巯基乙醇 、 sodium chloride 、 calcium chloride 作用下， 生成 benzyloxycarbonylmethyl (2S,3R)-3-tertbutyloxy-2-(((9H-fluoren-9-ylmethoxy)carbonyl)amino)butanoate
  参考文献：
  名称：

  Isopeptide Ligation Catalyzed by Quintessential Sortase A

  摘要：

  The housekeeping transpeptidase sortase A (SrtA) from Staphyloccocus aureus catalyzes the covalent anchoring of surface proteins to the cell wall by linking the threonyl carboxylate of the LPXTG recognition motif to the amino group of the pentaglycine cross-bridge of the peptidoglycan. SrtA-catalyzed ligation of an LPXTG containing polypeptide with an aminoglycine-terminated moiety occurs efficiently in vitro and has inspired the use of this enzyme as a synthetic tool in biological chemistry. Here we demonstrate the propensity of SrtA to catalyze "isopeptide" ligation. Using model peptide sequences, we show that SrtA can transfer LPXTG peptide substrates to the epsilon-amine of specific Lys residues and form cyclized and/or a gamut of branched oligomers. Our results provide insights about principles governing isopeptide ligation reactions catalyzed by SrtA and suggest that although cyclization is guided by distance relationship between Lys (epsilon-amine) and Thr (alpha-carboxyl) residues, facile branched oligomerization requires the presence of a stable and long-lived acyl-enzyme intermediate.

  DOI：

  10.1074/jbc.m111.247650
• 作为产物：
  描述：

  Fmoc-甘氨酸 、 Fmoc-L-亮氨酸 、 Fmoc-L-丙氨酸 、 Fmoc-L-脯氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 生成 YALPETGK
  参考文献：
  名称：

  Peptide−Sugar Ligation Catalyzed by Transpeptidase Sortase:  A Facile Approach to Neoglycoconjugate Synthesis

  摘要：

  Glycoconjugate synthesis involving sugar and polypeptide remains a formidable challenge. Here we report a novel enzymatic method involving an unprecedented sortase-catalyzed transamidation reaction for site-specific engineering of sugars into native proteins. We show that sugars appended with a 6-aminohexose moiety can be efficiently ligated to peptides; and proteins encoded with a LPXTG sortase, recognition sequence. This robust reaction provides an elegant and simple approach for generating neoglycoproteins with an amide-linked sugar moiety at the carboxy terminus.

  DOI：

  10.1021/ja077358g

文献信息

• Peptide−Sugar Ligation Catalyzed by Transpeptidase Sortase:  A Facile Approach to Neoglycoconjugate Synthesis
  作者：Sharmishtha Samantaray、Uttara Marathe、Sayani Dasgupta、Vinay K. Nandicoori、Rajendra P. Roy

  DOI：10.1021/ja077358g

  日期：2008.2.1

  Glycoconjugate synthesis involving sugar and polypeptide remains a formidable challenge. Here we report a novel enzymatic method involving an unprecedented sortase-catalyzed transamidation reaction for site-specific engineering of sugars into native proteins. We show that sugars appended with a 6-aminohexose moiety can be efficiently ligated to peptides; and proteins encoded with a LPXTG sortase, recognition sequence. This robust reaction provides an elegant and simple approach for generating neoglycoproteins with an amide-linked sugar moiety at the carboxy terminus.
• Isopeptide Ligation Catalyzed by Quintessential Sortase A
  作者：Sayani Dasgupta、Sharmishtha Samantaray、Dinkar Sahal、Rajendra P. Roy

  DOI：10.1074/jbc.m111.247650

  日期：2011.7

  The housekeeping transpeptidase sortase A (SrtA) from Staphyloccocus aureus catalyzes the covalent anchoring of surface proteins to the cell wall by linking the threonyl carboxylate of the LPXTG recognition motif to the amino group of the pentaglycine cross-bridge of the peptidoglycan. SrtA-catalyzed ligation of an LPXTG containing polypeptide with an aminoglycine-terminated moiety occurs efficiently in vitro and has inspired the use of this enzyme as a synthetic tool in biological chemistry. Here we demonstrate the propensity of SrtA to catalyze "isopeptide" ligation. Using model peptide sequences, we show that SrtA can transfer LPXTG peptide substrates to the epsilon-amine of specific Lys residues and form cyclized and/or a gamut of branched oligomers. Our results provide insights about principles governing isopeptide ligation reactions catalyzed by SrtA and suggest that although cyclization is guided by distance relationship between Lys (epsilon-amine) and Thr (alpha-carboxyl) residues, facile branched oligomerization requires the presence of a stable and long-lived acyl-enzyme intermediate.