α-1,2-L-arabinofuranobiose | 129022-49-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: α-1,2-L-arabinofuranobiose
• 英文别名: Ara(1->2)Ara；Araf(a1-2)a-Araf；(2R,3R,4S,5S)-3-[(2S,3R,4R,5S)-3,4-dihydroxy-5-(hydroxymethyl)oxolan-2-yl]oxy-5-(hydroxymethyl)oxolane-2,4-diol
• CAS: 129022-49-7
• 化学式: C₁₀H₁₈O₉
• 分子量: 282.248
• InChiKey: YKHKYDDELRYDNQ-DUDQFARASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.12
• 重原子数：
  19.0
• 可旋转键数：
  4.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  149.07
• 氢给体数：
  6.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  α-1,2-L-arabinofuranobiose 在 Streptomyces avermitilis exo-1,5-α-L-arabinofuranosidase, L289A mutant 作用下， 反应 2.0h， 生成 L-阿拉伯糖
  参考文献：
  名称：

  Crystal Structure of an Exo-1,5-α-l-arabinofuranosidase from Streptomyces avermitilis Provides Insights into the Mechanism of Substrate Discrimination between Exo- and Endo-type Enzymes in Glycoside Hydrolase Family 43*

  摘要：

  Exo-1,5-alpha-L-arabinofuranosidases belonging to glycoside hydrolase family 43 have strict substrate specificity. These enzymes hydrolyze only the alpha-1,5-linkages of linear arabinan and arabino-oligosaccharides in an exo-acting manner. The enzyme from Streptomyces avermitilis contains a core catalytic domain belonging to glycoside hydrolase family 43 and a C-terminal arabinan binding module belonging to carbohydrate binding module family 42. We determined the crystal structure of intact exo-1,5-alpha-L-arabinofuranosidase. The catalytic module is composed of a 5-bladed beta-propeller topologically identical to the other family 43 enzymes. The arabinan binding module had three similar subdomains assembled against one another around a pseudo-3-fold axis, forming a beta-trefoil-fold. A sugar complex structure with alpha-1,5-L-arabinofuranotriose revealed three subsites in the catalytic domain, and a sugar complex structure with alpha-L-arabinofuranosyl azide revealed three arabinose-binding sites in the carbohydrate binding module. A mutagenesis study revealed that substrate specificity was regulated by residues Asn-159, Tyr-192, and Leu-289 located at the aglycon side of the substrate-binding pocket. The exo-acting manner of the enzyme was attributed to the strict pocket structure of subsite -1, formed by the flexible loop region Tyr-281-Arg-294 and the side chain of Tyr-40, which occupied the positions corresponding to the catalytic glycon cleft of GH43 endo-acting enzymes.

  DOI：

  10.1074/jbc.m110.164251