4-nitrophenyl 1,4-β-D-thiogalactobioside | 1338073-21-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 4-nitrophenyl 1,4-β-D-thiogalactobioside
• CAS: 1338073-21-4
• 化学式: C₁₈H₂₅NO₁₂S
• 分子量: 479.462
• InChiKey: SOVDTKNEMFCCRR-BQVHMPCVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.69
• 重原子数：
  32.0
• 可旋转键数：
  7.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  212.44
• 氢给体数：
  7.0
• 氢受体数：
  13.0

反应信息

• 作为反应物：
  描述：

  4-nitrophenyl 1,4-β-D-thiogalactobioside 在 水 作用下， 生成
  参考文献：
  名称：

  Activity of three β-1,4-galactanases on small chromogenic substrates

  摘要：

  beta-1,4-Galactanases belong to glycoside hydrolase family GH 53 and degrade galactan and arabinogalactan side chains of the complex pectin network in plant cell walls. Two fungal beta-1,4-galactanases from Aspergillus aculeatus, Meripileus giganteus and one bacterial enzyme from Bacillus licheniformis have been kinetically characterized using the chromogenic substrate analog 4-nitrophenyl beta-1,4-D-thiogalactobioside synthesized by the thioglycoligase approach. Values of k(cat)/K-m for this substrate with A. aculeatus beta-1,4-galactanase at pH 4.4 and for M. giganteus beta-1,4-galactanase at pH 5.5 are 333 M (1) s (1) and 62 M (1) s (1), respectively. By contrast the B. licheniformis beta-1,4-galactanase did not hydrolyze 4-nitrophenyl beta-1,4-D-thiogalactobioside. The different kinetic behavior observed between the two fungal and the bacterial beta-1,4-galactanases can be ascribed to an especially long loop 8 observed only in the structure of B. licheniformis beta-1,4-galactanase. This loop contains substrate binding subsites -3 and -4, which presumably cause B. licheniformis beta-1,4-galactanase to bind 4-nitrophenyl -1,4-beta-D-thiogalactobioside non-productively. In addition to their cleavage of 4-nitrophenyl -1,4-beta-D-thiogalactobioside, the two fungal enzymes also cleaved the commercially available 2-nitrophenyl-1,4-beta-D-galactopyranoside, but kinetic parameters could not be determined because of transglycosylation at substrate concentrations above 4 mM. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2011.05.017
• 作为产物：
  描述：

  2',4'-二硝基苯基-beta-吡喃半乳糖苷 、 4-nitrophenyl 4-deoxy-4-thio-β-D-galactopyranoside 在 mutant Agrobacterium sp. β-glucosidase E170G 作用下， 反应 25.0h， 生成 4-nitrophenyl 1,4-β-D-thiogalactobioside
  参考文献：
  名称：

  Activity of three β-1,4-galactanases on small chromogenic substrates

  摘要：

  beta-1,4-Galactanases belong to glycoside hydrolase family GH 53 and degrade galactan and arabinogalactan side chains of the complex pectin network in plant cell walls. Two fungal beta-1,4-galactanases from Aspergillus aculeatus, Meripileus giganteus and one bacterial enzyme from Bacillus licheniformis have been kinetically characterized using the chromogenic substrate analog 4-nitrophenyl beta-1,4-D-thiogalactobioside synthesized by the thioglycoligase approach. Values of k(cat)/K-m for this substrate with A. aculeatus beta-1,4-galactanase at pH 4.4 and for M. giganteus beta-1,4-galactanase at pH 5.5 are 333 M (1) s (1) and 62 M (1) s (1), respectively. By contrast the B. licheniformis beta-1,4-galactanase did not hydrolyze 4-nitrophenyl beta-1,4-D-thiogalactobioside. The different kinetic behavior observed between the two fungal and the bacterial beta-1,4-galactanases can be ascribed to an especially long loop 8 observed only in the structure of B. licheniformis beta-1,4-galactanase. This loop contains substrate binding subsites -3 and -4, which presumably cause B. licheniformis beta-1,4-galactanase to bind 4-nitrophenyl -1,4-beta-D-thiogalactobioside non-productively. In addition to their cleavage of 4-nitrophenyl -1,4-beta-D-thiogalactobioside, the two fungal enzymes also cleaved the commercially available 2-nitrophenyl-1,4-beta-D-galactopyranoside, but kinetic parameters could not be determined because of transglycosylation at substrate concentrations above 4 mM. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2011.05.017