α-L-arabinofuranosyl azide | 1258782-90-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: α-L-arabinofuranosyl azide
• 英文别名: (2R,3R,4R,5S)-2-azido-5-(hydroxymethyl)tetrahydrofuran-3,4-diol；(2R,3R,4R,5S)-2-azido-5-(hydroxymethyl)oxolane-3,4-diol
• CAS: 1258782-90-9
• 化学式: C₅H₉N₃O₄
• 分子量: 175.144
• InChiKey: DHFFHQUOZLQWBU-QMKXCQHVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  84.3
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  2,3,5-tribenzoyl-α-L-arabinofuranosyl azide 在 sodium methylate 作用下， 以 甲醇 为溶剂， 反应 2.0h， 以100%的产率得到α-L-arabinofuranosyl azide
  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

文献信息

• Mechanism-based inhibition of GH127/146 cysteine glycosidases by stereospecifically functionalized l-arabinofuranosides
  作者：Akihiro Ishiwata、Satoru Narita、Kenta Kimura、Katsunori Tanaka、Kiyotaka Fujita、Shinya Fushinobu、Yukishige Ito

  DOI：10.1016/j.bmc.2022.117054

  日期：2022.12

  To understand the precise mechanism of the glycoside hydrolase (GH) family 127, a cysteine β-l-arabinofuranosidase (Arafase) – HypBA1 – has been isolated from Bifidobacterium longum in the human Gut microbiota, and the design and synthesis of the mechanism-based inhibitors such as l-Araf-haloacetamides have been carried out. The α-l-Araf-azide derivative was used as the monoglycosylamine equivalent

  为了了解糖苷水解酶 (GH) 家族 127 的精确机制，从人类肠道菌群中的长双歧杆菌中分离出了半胱氨酸 β- l -阿拉伯呋喃糖苷酶 (Ara f ase) – HypBA1，并设计和合成了该机制基于α-的抑制剂例如l -Ara f-卤代乙酰胺已经被开发出来。 α- l -Ara f-叠氮化物衍生物用作单糖胺等价物，以高度立体选择性提供l -Ara f-氯乙酰胺（α/β- 1 -Cl）以及溴乙酰胺（α/β- 1 -Br）通过施陶丁格反应，然后在有/无异构化的情况下形成酰胺。针对HypBA1，探针1 ，特别是在α/β- 1 -Br的情况下抑制水解。本手稿讨论了这些观察结果的构象含义。使用l -Ara f-叠氮化物 (α/β- 5 ) 进行的额外检查对 GH127/146 半胱氨酸糖苷酶进行了进一步的机制观察，包括作为底物的 β- 5的水解和使用 GH127 同系物的 α- 5的氧化抑制。