N-methoxyacetate-D-mannosamine

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-methoxyacetate-D-mannosamine
• 英文别名: N-methoxyacetyl-D-mannosamine；N-methylglycolyl mannosamine；ManNAcOMe；ManNGcMe；2-methoxy-N-[(3S,4R,5S,6R)-2,4,5-trihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide
• 化学式: C₉H₁₇NO₇
• 分子量: 251.236
• InChiKey: OTCILNIJZXPDNB-TVCQNHEDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.8
• 重原子数：
  17
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  129
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  N-methoxyacetate-D-mannosamine 、 sodium pyruvate 、 3-azidopropyl β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside 在 E_.coli K₁₂ sialic acid aldolase 、 N_.meningitidis CMP-Sia synthetase tPm₀₁₈₈Ph 、 胞苷-5’-三磷酸 、 magnesium chloride 作用下， 以 various solvents 为溶剂， 反应 2.0h， 以90%的产率得到3-azidopropyl O-(5-methoxyacetamido-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid)-(2->3)-O-β-D-galactopyranosyl-(1->4)-β-D-glucopyranoside
  参考文献：
  名称：

  A Multifunctional Pasteurella multocida Sialyltransferase:  A Powerful Tool for the Synthesis of Sialoside Libraries

  摘要：

  A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an alpha2,3-sialyltransferase (main function), (2) an alpha2,6-sialyltransferase, (3) an alpha2,3-sialidase, and (4) an alpha2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.

  DOI：

  10.1021/ja0561690
• 作为产物：
  描述：

  D-mannosamine hydrochloride 、 2,5-吡咯烷二酮,1-[(甲氧基乙酰基)氧代]- 在 三乙胺 作用下， 以 甲醇 为溶剂， 以92%的产率得到N-methoxyacetate-D-mannosamine
  参考文献：
  名称：

  A Multifunctional Pasteurella multocida Sialyltransferase:  A Powerful Tool for the Synthesis of Sialoside Libraries

  摘要：

  A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an alpha2,3-sialyltransferase (main function), (2) an alpha2,6-sialyltransferase, (3) an alpha2,3-sialidase, and (4) an alpha2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.

  DOI：

  10.1021/ja0561690

文献信息

• Sialidase substrate specificity studies using chemoenzymatically synthesized sialosides containing C5-modified sialic acids
  作者：Hongzhi Cao、Yanhong Li、Kam Lau、Saddam Muthana、Hai Yu、Jiansong Cheng、Harshal A. Chokhawala、Go Sugiarto、Lei Zhang、Xi Chen

  DOI：10.1039/b916305k

  日期：——

  para-Nitrophenol-tagged sialyl galactosides containing sialic acid derivatives in which the C5 hydroxyl group of sialic acids was systematically substituted with a hydrogen, a fluorine, a methoxyl or an azido group were successfully synthesized using an efficient chemoenzymatic approach. These compounds were used as valuable probes in high-throughput screening assays to study the importance of the C5 hydroxyl group of sialic acid in the recognition and the cleavage of sialoside substrates by bacterial sialidases.

  成功合成了标记有对硝基苯酚的含唾液酸衍生物的唾液酸半乳糖苷，这些衍生物中唾液酸的C5羟基以氢、氟、甲氧基或叠氮基进行了系统性的替代，采用了一种高效的化学酶法。这些化合物作为宝贵的探针，用于高通量筛选实验，研究了唾液酸C5羟基在细菌唾液酶识别和切割唾液苷底物中的重要性。
• Efficient chemoenzymatic synthesis of sialyl Tn-antigens and derivatives
  作者：Li Ding、Hai Yu、Kam Lau、Yanhong Li、Saddam Muthana、Junru Wang、Xi Chen

  DOI：10.1039/c1cc12732b

  日期：——

  An N-terminal and C-terminal truncated recombinant α2–6-sialyltransferase cloned from Photobacterium sp. JH-ISH-224, Psp2,6ST(15–501)-His6, was shown to be an efficient catalyst for one-pot three-enzyme synthesis of sialyl Tn (STn) antigens and derivatives containing natural and non-natural sialic acid forms.

  从发光杆菌属克隆的 N 端和 C 端截短的重组 α2-6-唾液酸转移酶。 JH-ISH-224, Psp2,6ST(15–501)-His6，被证明是一锅三酶合成唾液酸 Tn (STn) 抗原和含有天然和非天然唾液酸形式的衍生物的有效催化剂。
• Chemoenzymatic Synthesis of GD3 Oligosaccharides and Other Disialyl Glycans Containing Natural and Non-natural Sialic Acids
  作者：Hai Yu、Jiansong Cheng、Li Ding、Zahra Khedri、Yi Chen、Sharlene Chin、Kam Lau、Vinod Kumar Tiwari、Xi Chen

  DOI：10.1021/ja907750r

  日期：2009.12.30

  occurring sialic acid variations on disialyl structures in nature, we developed an efficient two-step multienzyme approach for the synthesis of a series of GD3 ganglioside oligosaccharides and other disialyl glycans containing a terminal Siaalpha2-8Sia component with different natural and non-natural sialic acids. In the first step, alpha2-3- or alpha2-6-linked monosialylated oligosaccharides were obtained

  为了了解自然界中二唾液酸结构上天然存在的唾液酸变异的生物学重要性，我们开发了一种有效的两步多酶方法来合成一系列 GD3 神经节苷脂寡糖和其他含有末端 Siaalpha2-8Sia 组分的二唾液酸聚糖不同的天然和非天然唾液酸。在第一步中，使用一锅三酶方法获得了 alpha2-3-或 alpha2-6-连接的单唾液酸化寡糖。然后将这些化合物用作受体，用于重组截短的多功能空肠弯曲杆菌唾液酸转移酶 CstII 突变体 CstIIDelta32(I53S) 的 alpha2-8-唾液酸转移酶活性，以生产二唾液酸寡糖。CstIIDelta32(I53S) 的 alpha2-8-唾液酸转移酶活性具有混杂的供体底物特异性，可以容忍 CMP 唾液酸中唾液酸 C-5 或 C-9 处的各种替换，而其受体底物特异性相对受到限制。可接受的单唾液酸化寡糖受体中的末端唾液酸残基仅限于 Neu5Ac、Neu5Gc、KDN
• Highly Efficient Chemoenzymatic Synthesis of Naturally Occurring and Non-Natural α-2,6-Linked Sialosides: AP. damsela α-2,6-Sialyltransferase with Extremely Flexible Donor–Substrate Specificity
  作者：Hai Yu、Shengshu Huang、Harshal Chokhawala、Mingchi Sun、Haojie Zheng、Xi Chen

  DOI：10.1002/anie.200600572

  日期：2006.6.12
• A Multifunctional <i>Pasteurella multocida</i> Sialyltransferase:  A Powerful Tool for the Synthesis of Sialoside Libraries
  作者：Hai Yu、Harshal Chokhawala、Rebekah Karpel、Hui Yu、Bingyuan Wu、Jianbo Zhang、Yingxin Zhang、Qiang Jia、Xi Chen

  DOI：10.1021/ja0561690

  日期：2005.12.1

  A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an alpha2,3-sialyltransferase (main function), (2) an alpha2,6-sialyltransferase, (3) an alpha2,3-sialidase, and (4) an alpha2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.