BOC-Lys(Z)-NH2 | 106326-22-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: BOC-Lys(Z)-NH2
• 英文别名: benzyl N-[(5R)-6-amino-5-[(2-methylpropan-2-yl)oxycarbonylamino]-6-oxohexyl]carbamate
• CAS: 106326-22-1
• 化学式: C₁₉H₂₉N₃O₅
• 分子量: 379.456
• InChiKey: DAJHIUICHSIAAV-OAHLLOKOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  27
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  120
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  BOC-Lys(Z)-NH2 在 20% palladium hydroxide-activated charcoal 、 氢气 作用下， 以 甲醇 为溶剂， 反应 1.5h， 生成 N-(叔丁氧羰基)-D-赖氨酸
  参考文献：
  名称：

  Reconstitution of Peptidoglycan Cross-Linking Leads to Improved Fluorescent Probes of Cell Wall Synthesis

  摘要：

  The peptidoglycan precursor, Lipid II, produced in the model Gram-positive bacterium Bacillus subtilis differs from Lipid II found in Gram-negative bacteria such as Escherichia coli by a single amidation on the peptide side chain. How this difference affects the cross-linking activity of penicillin-binding proteins (PBPs) that assemble peptidoglycan in cells has not been investigated because B. subtilis Lipid II was not previously available. Here we report the synthesis of B. subtilis Lipid II and its use by purified B. subtilis PBP1 and E. coli PBP1A. While enzymes from both organisms assembled B. subtilis Lipid II into glycan strands, only the B. subtilis enzyme cross-linked the strands. Furthermore, B. subtilis PBP1 catalyzed the exchange of both D-amino acids and D-amino carboxamides into nascent peptidoglycan, but the E. coli enzyme only exchanged n-amino acids. We exploited these observations to design a fluorescent n-amino carboxamide probe to label B. subtilis PG in vivo and found that this probe labels the cell wall dramatically better than existing reagents.

  DOI：

  10.1021/ja505668f
• 作为产物：
  描述：

  N2-[叔丁氧羰基]-N6-[苄氧羰基]-D-赖氨酸 在 N,N'-羰基二咪唑 、 氨 作用下， 以 N,N-二甲基甲酰胺 、 水 为溶剂， 反应 7.5h， 以380 mg的产率得到BOC-Lys(Z)-NH2
  参考文献：
  名称：

  Reconstitution of Peptidoglycan Cross-Linking Leads to Improved Fluorescent Probes of Cell Wall Synthesis

  摘要：

  The peptidoglycan precursor, Lipid II, produced in the model Gram-positive bacterium Bacillus subtilis differs from Lipid II found in Gram-negative bacteria such as Escherichia coli by a single amidation on the peptide side chain. How this difference affects the cross-linking activity of penicillin-binding proteins (PBPs) that assemble peptidoglycan in cells has not been investigated because B. subtilis Lipid II was not previously available. Here we report the synthesis of B. subtilis Lipid II and its use by purified B. subtilis PBP1 and E. coli PBP1A. While enzymes from both organisms assembled B. subtilis Lipid II into glycan strands, only the B. subtilis enzyme cross-linked the strands. Furthermore, B. subtilis PBP1 catalyzed the exchange of both D-amino acids and D-amino carboxamides into nascent peptidoglycan, but the E. coli enzyme only exchanged n-amino acids. We exploited these observations to design a fluorescent n-amino carboxamide probe to label B. subtilis PG in vivo and found that this probe labels the cell wall dramatically better than existing reagents.

  DOI：

  10.1021/ja505668f

文献信息

• GOTO, GIITI;NAGAOKA, AKINOBU;VAKIMASU, MITSUXIRO
  作者：GOTO, GIITI、NAGAOKA, AKINOBU、VAKIMASU, MITSUXIRO

  DOI：——

  日期：——
• SALVADORI, S.;MARASTONI, M.;BALBONI, G.;TOMATIS, R.;BOREA, P. A., FARMACO. ED. SCI., 42,(1987) N 12, 931-940
  作者：SALVADORI, S.、MARASTONI, M.、BALBONI, G.、TOMATIS, R.、BOREA, P. A.

  DOI：——

  日期：——
• GOTO, GLICHI;NAGAOKA, AKINOBU;WAKIMASU, MITSUHIRO
  作者：GOTO, GLICHI、NAGAOKA, AKINOBU、WAKIMASU, MITSUHIRO

  DOI：——

  日期：——
• Reconstitution of Peptidoglycan Cross-Linking Leads to Improved Fluorescent Probes of Cell Wall Synthesis
  作者：Matthew D. Lebar、Janine M. May、Alexander J. Meeske、Sara A. Leiman、Tania J. Lupoli、Hirokazu Tsukamoto、Richard Losick、David Z. Rudner、Suzanne Walker、Daniel Kahne

  DOI：10.1021/ja505668f

  日期：2014.8.6

  The peptidoglycan precursor, Lipid II, produced in the model Gram-positive bacterium Bacillus subtilis differs from Lipid II found in Gram-negative bacteria such as Escherichia coli by a single amidation on the peptide side chain. How this difference affects the cross-linking activity of penicillin-binding proteins (PBPs) that assemble peptidoglycan in cells has not been investigated because B. subtilis Lipid II was not previously available. Here we report the synthesis of B. subtilis Lipid II and its use by purified B. subtilis PBP1 and E. coli PBP1A. While enzymes from both organisms assembled B. subtilis Lipid II into glycan strands, only the B. subtilis enzyme cross-linked the strands. Furthermore, B. subtilis PBP1 catalyzed the exchange of both D-amino acids and D-amino carboxamides into nascent peptidoglycan, but the E. coli enzyme only exchanged n-amino acids. We exploited these observations to design a fluorescent n-amino carboxamide probe to label B. subtilis PG in vivo and found that this probe labels the cell wall dramatically better than existing reagents.