m-tolyl-α-D-glucopyranoside | 3150-23-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: m-tolyl-α-D-glucopyranoside
• 英文别名: m-Tolyl-α-D-glucopyranosid；m-Kresol-α-D-glucopyranosid；m-Tolyl-α-D-glucopyranosid；m-Tolyl-alpha-glucoside；(2R,3S,4S,5R,6R)-2-(hydroxymethyl)-6-(3-methylphenoxy)oxane-3,4,5-triol
• CAS: 3150-23-0；6092-25-7；19887-83-3；25678-11-9；28541-81-3；89731-59-9
• 化学式: C₁₃H₁₈O₆
• 分子量: 270.282
• InChiKey: QCLIKCCGRQFFHT-LBELIVKGSA-N

物化性质

• 熔点：
  166-168 °C
• 沸点：
  496.2±45.0 °C(Predicted)
• 密度：
  1.401±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  19
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.54
• 拓扑面积：
  99.4
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  3-methylphenyl 2,3,4,6-tetra-O-acetyl-α-D-glucopyranoside 在 甲醇 、 sodium methylate 作用下， 生成 m-tolyl-α-D-glucopyranoside
  参考文献：
  名称：

  Kariyone et al., Yakugaku Zasshi/Journal of the Pharmaceutical Society of Japan, 1952, vol. 72, p. 13

  摘要：

  DOI：

文献信息

• Purification, characterization, and gene identification of an α-glucosyl transfer enzyme, a novel type α-glucosidase from Xanthomonas campestris WU-9701
  作者：Toshiyuki Sato、Nobukazu Hasegawa、Jun Saito、Satoru Umezawa、Yuki Honda、Kuniki Kino、Kohtaro Kirimura

  DOI：10.1016/j.molcatb.2012.04.014

  日期：2012.8

  The alpha-glucosyl transfer enzyme (XgtA), a novel type alpha-glucosidase produced by Xanthomonas campestris WU-9701, was purified from the cell-free extract and characterized. The molecular weight of XgtA is estimated to be 57 kDa by SOS-PAGE and 60 kDa by gel filtration, indicating that XgtA is a monomeric enzyme. Kinetic properties of XgtA were determined for alpha-glucosyl transfer and maltose-hydrolyzing activities using maltose as the alpha-glucosyl donor, and if necessary, hydroquinone as the acceptor. The V-max value for alpha-glucosyl transfer activity was 1.3 x 10(-2) (mM/s); this value was 3.9-fold as much as that for maltose-hydrolyzing activity. XgtA neither produced maltooligosaccharides nor hydrolyzed sucrose. The gene encoding XgtA that contained a 1614-bp open reading frame was cloned, identified, and highly expressed in Escherichia coli JM109 as the host. Site-directed mutagenesis identified Asp201,Glu270, and Asp331 as the catalytic sites of XgtA, indicating that XgtA belongs to the glycoside hydrolase family 13. (C) 2012 Elsevier B.V. All rights reserved.
• Helferich; Johannis, Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, 1960, vol. 320, p. 75,79
  作者：Helferich、Johannis

  DOI：——

  日期：——
• Hall et al., Journal of the Chemical Society, 1961, p. 4294
  作者：Hall et al.

  DOI：——

  日期：——
• Kariyone et al., Yakugaku Zasshi/Journal of the Pharmaceutical Society of Japan, 1952, vol. 72, p. 13
  作者：Kariyone et al.

  DOI：——

  日期：——