| 174231-06-2

• 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
• CAS: 174231-06-2
• 化学式: C₁₇H₂₀N₂O₆S
• 分子量: 380.422
• InChiKey: BDQRPOOKPMVAJW-JVBMTESESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  26.0
• 可旋转键数：
  5.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  109.98
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  在 palladium on activated charcoal 氢气 作用下， 以62%的产率得到(5R)-6c-((R)-1-hydroxy-ethyl)-3,3-dimethyl-7-oxo-(5rH)-4-thia-1-aza-bicyclo[3.2.0]heptane-2c-carboxylic acid
  参考文献：
  名称：

  Quantification of the extent of attenuation of the rate of turnover chemistry of the TEM-1 β-lactamase by the α-1R-hydroxyethyl group in substrates

  摘要：

  The 6 alpha-1R-hydroxyethyl group of imipenem, a clinically used carbapenem antibacterial agent, is believed to displace the hydrolytic water from its optimal position in the active site of class A beta-lactamases. This interaction renders the molecule a poor substrate for these bacterial enzymes, hence preserving the antibacterial property of the antibiotic. The extent of the contribution of the 6 alpha-1R-hydroxyethyl group in substrates toward stabilization of the antibiotic to the hydrolytic action of class A TEM-1 beta-lactamase was studied by the synthesis and evaluation of two penicillanic acid derivatives, 6 alpha-(1R-hydroxyethyl)penicillanic acid (2) and 6 beta-(1R-hydroxyethyl)penicillanic acid (3). The kinetic evaluation of the enzymic hydrolysis of these two penicillanic acid derivatives indicated that the 6 alpha-1R-hydroxyethyl group imparts as much as 10(4)-fold to the hydrolytic stability of the beta-lactam substrate.

  DOI：

  10.1016/0960-894x(96)00022-4
• 作为产物：
  描述：

  4-Nitrobenzyl 6,6-dibromopenicillanate 在 偶氮二异丁腈 、 甲基溴化镁 、 三正丁基氢锡 作用下， 生成
  参考文献：
  名称：

  Quantification of the extent of attenuation of the rate of turnover chemistry of the TEM-1 β-lactamase by the α-1R-hydroxyethyl group in substrates

  摘要：

  The 6 alpha-1R-hydroxyethyl group of imipenem, a clinically used carbapenem antibacterial agent, is believed to displace the hydrolytic water from its optimal position in the active site of class A beta-lactamases. This interaction renders the molecule a poor substrate for these bacterial enzymes, hence preserving the antibacterial property of the antibiotic. The extent of the contribution of the 6 alpha-1R-hydroxyethyl group in substrates toward stabilization of the antibiotic to the hydrolytic action of class A TEM-1 beta-lactamase was studied by the synthesis and evaluation of two penicillanic acid derivatives, 6 alpha-(1R-hydroxyethyl)penicillanic acid (2) and 6 beta-(1R-hydroxyethyl)penicillanic acid (3). The kinetic evaluation of the enzymic hydrolysis of these two penicillanic acid derivatives indicated that the 6 alpha-1R-hydroxyethyl group imparts as much as 10(4)-fold to the hydrolytic stability of the beta-lactam substrate.

  DOI：

  10.1016/0960-894x(96)00022-4

文献信息

• Stereoselective Reduction of α-Bromopenicillanates by Tributylphosphine
  作者：Akihiro Ishiwata、Lakshmi P. Kotra、Kazuyuki Miyashita、Tsuyoshi Nagase、Shahriar Mobashery

  DOI：10.1021/ol000185e

  日期：2000.9.1

  [reaction: see text] Diastereoselective reduction of 6-bromo-6-substituted penicillanate esters has been achieved by treatment with tributylphosphine to give 6-substituted penicillanate esters. This reaction would appear to proceed through a phosphonium beta-lactam enolate species, followed by a diastereoselective protonation. This method has the advantage of being simple to carry out and it is mild

  [反应：见正文]通过用三丁基膦处理得到6-取代的青霉酸酯，已经实现了6-溴-6-取代的青霉酸酯的非对映选择性还原。该反应似乎通过through-β-内酰胺烯醇化species物种进行，随后是非对映选择性质子化。该方法的优点是易于实施，并且温和，非对映选择性高，并且应能耐受底物中的许多官能团。这些意见的含义进行了讨论。
• Synthesis and biological evaluation of penem inhibitors of bacterial signal peptidase
  作者：David A. Harris、Michael E. Powers、Floyd E. Romesberg

  DOI：10.1016/j.bmcl.2009.04.034

  日期：2009.7

  We report the first synthesis of a 5S penem, known to bind bacterial type I signal peptidase, from the commercially available and inexpensive 6-aminopenicillanic acid. We report the first in vivo activity of the compound and use structure-activity relationship studies to begin to define the determinants of signal peptidase binding and also to begin to optimize the penem as an antibiotic. (C) 2009 Elsevier Ltd. All rights reserved.