L-galactonic acid

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羟基酸及其衍生物
• 英文名称: L-galactonic acid
• 英文别名: L-Galactonsaeure；L-galacto-2,3,4,5,6-Pentahydroxy-hexansaeure；L-Galaktonsaeure；(2S,3R,4R,5S)-2,3,4,5,6-pentahydroxyhexanoic acid
• 化学式: C₆H₁₂O₇
• 分子量: 196.157
• InChiKey: RGHNJXZEOKUKBD-RSJOWCBRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.4
• 重原子数：
  13
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  138
• 氢给体数：
  6
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  L-galactonic acid 在 吡啶 、 sodium amalgam 、 乙醇 、 硫酸 、 水 作用下， 生成 L(-)-塔洛糖
  参考文献：
  名称：

  我-塔洛斯

  摘要：

  DOI：

  10.1002/hlca.19380210101
• 作为产物：
  描述：

  L-(-)-半乳糖 在 溴 作用下， 生成 L-galactonic acid
  参考文献：
  名称：

  van Ekenstein; Blanksma, Chemisches Zentralblatt, 1914, vol. 85, # I, p. 965

  摘要：

  DOI：

文献信息

• Functional Characterization of<scp>D</scp>-Galacturonic Acid Reductase, a Key Enzyme of the Ascorbate Biosynthesis Pathway, from<i>Euglena gracilis</i>
  作者：Takahiro ISHIKAWA、Ikuko MASUMOTO、Naofumi IWASA、Hitoshi NISHIKAWA、Yoshihiro SAWA、Hitoshi SHIBATA、Ayana NAKAMURA、Yukinori YABUTA、Shigeru SHIGEOKA

  DOI：10.1271/bbb.60327

  日期：2006.11.23

  D-Galacturonic acid reductase, a key enzyme in ascorbate biosynthesis, was purified to homogeneity from Euglena gracilis. The enzyme was a monomer with a molecular mass of 38-39 kDa, as judged by SDS-PAGE and gel filtration. Apparently it utilized NADPH with a Km value of 62.5+/-4.5 microM and uronic acids, such as D-galacturonic acid (Km=3.79+/-0.5 mM) and D-glucuronic acid (Km=4.67+/-0.6 mM). It

  D-Galacturonic酸还原酶是抗坏血酸生物合成中的关键酶，可从细叶藻（Euglena gracilis）中纯化至同质。通过SDS-PAGE和凝胶过滤判断，该酶是分子量为38-39kDa的单体。显然，它利用Km值为62.5 +/- 4.5 microM的NADPH和糖醛酸，例如D-半乳糖醛酸（Km = 3.79 +/- 0.5 mM）和D-葡萄糖醛酸（Km = 4.67 +/- 0.6 mM） 。它未能催化与L-半乳糖酸和NADP（+）的逆反应。还原D-半乳糖醛酸的最佳pH为7.2。该酶被0.1 mM H（2）O（2）激活了45.6％，表明该酶的活性受细胞氧化还原状态的调节。没有观察到L-半乳糖-1,4-内酯或抗坏血酸对酶活性的反馈调节。
• Dually derivatized chitosan nanoparticles and methods of making and using the same for gene transfer in vivo
  申请人：ENGENE, INC.

  公开号：US10456481B2

  公开（公告）日：2019-10-29

  Provided herein is chitosan-derivative nanoparticle comprising chitosan functionalized with a cationic amino acid and a hydrophilic polyol; and methods of making and using same, e.g., for gene delivery in vivo.

  本文提供了壳聚糖衍生物纳米粒子，包括用阳离子氨基酸和亲水多元醇官能化的壳聚糖；以及制造和使用这种纳米粒子的方法，例如用于体内基因递送。
• Ault et al., Journal of the Chemical Society, 1933, p. 1419,1422
  作者：Ault et al.

  DOI：——

  日期：——
• Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives
  作者：Yang Zou、Wenjun Wang、Li Cai、Leilei Chen、Mengyang Xue、Xiaomei Zhang、Jie Shen、Min Chen

  DOI：10.1016/j.bmcl.2012.03.095

  日期：2012.5

  Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate L-mannose in moderate yield (43%), while other L-sugars such as L-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as L-mannose. (C) 2012 Elsevier Ltd. All rights reserved.
• Development of a Novel Biocatalyst for the Resolution ofrac-Pantolactone
  作者：Maria Kesseler、Thomas Friedrich、Hans Wolfgang Höffken、Bernhard Hauer

  DOI：10.1002/1615-4169(200212)344:10<1103::aid-adsc1103>3.0.co;2-r

  日期：2002.12

  A novel L-pantolactone hydrolase, Lph, from Agrobacterium tumefaciens Lu681 was characterized, which stereospecifically hydrolyseS L-pantolactone to L-pantoic acid yielding D-pantolactone with > 95% enantiomeric excess. The enzyme was found to be a 30 kDa-Zn2+-hydrolase with a K-m for L-pantolactone of 7 mM and a V-max of 30 U/mg. The corresponding lph gene was identified as an 807 bp ORF and cloned into E. coli. It was overexpressed under control of P-tac and P-rha yielding enzyme activities of up to 600 U/g dry weight. Resolution of D,L-pantolactone in repeated batches with isolated Lph and enzyme recovery by membrane filtration gave D-pantolactone with 50% yield and 90-95% ee over 6 days. Covalent immobilization to EupergitC led to a stable biocatalyst easy to handle in a repeated batch production of D-pantolactone. Further improvements in the activity of Lph were achieved by directed evolution of the enzyme. Activities of mutants F62S, K197D and F100L were increased 2.3, 1.7, and 1.5 fold, respectively.