UDP-α-D-galactosamine disodium salt | 137848-39-6

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: UDP-α-D-galactosamine disodium salt
• CAS: 137848-39-6
• 化学式: C₁₅H₂₃N₃O₁₆P₂*2Na
• 分子量: 609.285
• InChiKey: LWXNAZWQTLSQKD-AMKQWFBQSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -9.09
• 重原子数：
  37.0
• 可旋转键数：
  9.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  308.44
• 氢给体数：
  7.0
• 氢受体数：
  18.0

反应信息

• 作为反应物：
  描述：

  4-戊炔酸琥珀亚胺酯 、 UDP-α-D-galactosamine disodium salt 在 Bio-Rad AG 50W-X₈ resin (sodium form) 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 以52%的产率得到
  参考文献：
  名称：

  Engineering Orthogonal Polypeptide GalNAc-Transferase and UDP-Sugar Pairs

  摘要：

  O-Linked alpha-N-acetylgalactosamine (O-GalNAc) glycans constitute a major part of the human glycome. They are difficult to study because of the complex interplay of 20 distinct glycosyltransferase isoenzymes that initiate this form of glycosylation, the polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). Despite proven disease relevance, correlating the activity of individual GalNAc-Ts with biological function remains challenging due to a lack of tools to probe their substrate specificity in a complex biological environment. Here, we develop a "bump-hole" chemical reporter system for studying GalNAc-T activity in vitro. Individual GalNAc-Ts were rationally engineered to contain an enlarged active site (hole) and probed with a newly synthesized collection of 20 (bumped) uridine diphosphate N-acetylgalactosamine (UDP-GalNAc) analogs to identify enzyme-substrate pairs that retain peptide specificities but are otherwise completely orthogonal to native enzyme-substrate pairs. The approach was applicable to multiple GalNAc-T isoenzymes, including GalNAc-T1 and -T2 that prefer nonglycosylated peptide substrates and GalNAcT-10 that prefers a preglycosylated peptide substrate. A detailed investigation of enzyme kinetics and specificities revealed the robustness of the approach to faithfully report on GalNAc-T activity and paves the way for studying substrate specificities in living systems.

  DOI：

  10.1021/jacs.9b04695
• 作为产物：
  描述：

  uridine 5'-triphosphate trisodium salt 、 galactosamine-α-1-phosphate barium salt 在 sodium,[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl [hydroxy-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyphosphoryl] phosphate 作用下， 生成 UDP-α-D-galactosamine disodium salt
  参考文献：
  名称：

  Practical enzyme-based syntheses of uridine 5'-diphosphogalactose and uridine 5'-diphospho-N-acetylgalactosamine on a gram scale

  摘要：

  Practical enzyme-based routes for the syntheses of uridine 5'-diphosphogalactose (UDP-Gal) and uridine 5'-diphospho-N-acetylgalactosamine (UDP-GalNAc) on millimole scales have been developed. The activity of galactokinase (EC 2.7.1.6) in crude enzyme extracts from galactose-adapted yeast, coupled to a regenerating system for ATP, provides convenient and economical access to galactose-alpha-1-phosphate (Gal-1-P) and galactosamine-alpha-1-phosphate (GalN-1-P). The transfer of UMP to the sugar-1-phosphates was also accomplished enzymatically by Gal-1-P uridyltransferase (EC 2.7.7.12) using uridine 5'-diphosphoglucose (UDP-Glc) as the UMP donor. UDP-Glc was in turn regenerated in situ from glucose-1-phosphate and UTP using UDP-Glc pyrophosphorylase (EC 2.7.7.9). The only chemical step in the sequence was the acetylation of UDP-GalN to afford UDP-GalNAc using N-acetoxysuccinimide. The moderate overall yields (43% and 34% for UDP-Gal and UDP-GalNAc from Gal-1-P and GalN-1-P, respectively) were compensated by the straightforward preparation of the starting materials, UTP and the corresponding sugar-1-P.

  DOI：

  10.1021/jo00027a029