5-amino-5-deoxy-4-O-(β-D-glucopyranosyl)-D-glucono-1,5-lactam

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 5-amino-5-deoxy-4-O-(β-D-glucopyranosyl)-D-glucono-1,5-lactam
• 英文别名: (2r,3r,4r,5r)-4,5-Dihydroxy-2-(Hydroxymethyl)-6-Oxopiperidin-3-Yl Beta-D-Glucopyranoside；(3R,4R,5R,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxypiperidin-2-one
• 化学式: C₁₂H₂₁NO₁₀
• 分子量: 339.299
• InChiKey: WXSNJJDPPISYEF-ZNLUKOTNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.8
• 重原子数：
  23
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  189
• 氢给体数：
  8
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  2,3,6-tri-O-benzyl-4-O-(2,3,4,6-tetra-O-benzyl-β-D-glucopyranosyl)-D-glucono-1,5-lactone 在 palladium dihydroxide 氨 、 氢气 、 溶剂黄146 、 2-碘酰基苯甲酸 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 、 水 、 二甲基亚砜 为溶剂， 23.0~35.0 ℃ 、600.0 kPa 条件下， 反应 27.0h， 生成 5-amino-5-deoxy-4-O-(β-D-glucopyranosyl)-D-glucono-1,5-lactam
  参考文献：
  名称：

  Inhibition of Cellobiohydrolases fromTrichoderma reesei. Synthesis and Evaluation of Some Glucose-, Cellobiose-, and Cellotriose-Derived Hydroximolactams andImidazoles

  摘要：

  The lactam 16, the hydroximolactams 8, 20, 23, and 27, and the imidazole 32 were prepared following known methods. They were tested together with the known tetrazole 35 and the hydroximolactams 2 and 36 as inhibitors of the cellobiohydrolases Cel7A and Cel6A from Trichoderma reesei. Cel7A is only weakly inhibited by these compounds. Comparing their inhibitory activity evidences the importance of occupying subsites tl and +2. We results strongly suggest that the shape of none of the variants of the lactone-type inhibitor motif embodied by these inhibitors is complementary to the subsite - 1, i.e.,analogous to the transition state. Cel6A is rather strongly inhibited by the cellobiose analogues 20, 23, and 32, and by the cellotriose analogue 27. Their relative inhibitory activities evidence that binding at subsite -2 depends upon the shape of the moiety occupying subsite - 1. There is only a small difference between the inhibition by the hydroximolactams 20 and 23, which may be (partially) protonated by the catalytic acid of either anti- or syn-protonating glycosidases, and the imidazole 32, which can only be protonated by anti-protonating glycosidases. The results strongly suggest that shape requirements must be met by glycosidase inhibitors before they can be used to characterize the proton trajectory of glycosidases.

  DOI：

  10.1002/(sici)1522-2675(19990707)82:7<963::aid-hlca963>3.0.co;2-v

文献信息

• Inhibition of Cellobiohydrolases fromTrichoderma reesei. Synthesis and Evaluation of Some Glucose-, Cellobiose-, and Cellotriose-Derived Hydroximolactams andImidazoles
  作者：Stefan Vonhoff、Kathleen Piens、Muriel Pipelier、Christophe Braet、Marc Claeyssens、Andrea Vasella

  DOI：10.1002/(sici)1522-2675(19990707)82:7<963::aid-hlca963>3.0.co;2-v

  日期：1999.7.7

  The lactam 16, the hydroximolactams 8, 20, 23, and 27, and the imidazole 32 were prepared following known methods. They were tested together with the known tetrazole 35 and the hydroximolactams 2 and 36 as inhibitors of the cellobiohydrolases Cel7A and Cel6A from Trichoderma reesei. Cel7A is only weakly inhibited by these compounds. Comparing their inhibitory activity evidences the importance of occupying subsites tl and +2. We results strongly suggest that the shape of none of the variants of the lactone-type inhibitor motif embodied by these inhibitors is complementary to the subsite - 1, i.e.,analogous to the transition state. Cel6A is rather strongly inhibited by the cellobiose analogues 20, 23, and 32, and by the cellotriose analogue 27. Their relative inhibitory activities evidence that binding at subsite -2 depends upon the shape of the moiety occupying subsite - 1. There is only a small difference between the inhibition by the hydroximolactams 20 and 23, which may be (partially) protonated by the catalytic acid of either anti- or syn-protonating glycosidases, and the imidazole 32, which can only be protonated by anti-protonating glycosidases. The results strongly suggest that shape requirements must be met by glycosidase inhibitors before they can be used to characterize the proton trajectory of glycosidases.