N-[(2S,3S,5S)-3,5,6-trihydroxy-1-oxohexan-2-yl]acetamide

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-[(2S,3S,5S)-3,5,6-trihydroxy-1-oxohexan-2-yl]acetamide
• 化学式: C₈H₁₅NO₅
• 分子量: 205.211
• InChiKey: RPJFMDVQCIGBLX-RNJXMRFFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 重原子数：
  14
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  107
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  5-acetamido-3,5,7-trideoxy-D-galacto-2-nonulopyranosonic acid 在 L-lactate dehydrogenase 、 NauAc aldolase 、 还原型辅酶Ⅰ 作用下， 以 水 为溶剂， 生成 丙酮酸 、 N-[(2S,3S,5S)-3,5,6-trihydroxy-1-oxohexan-2-yl]acetamide
  参考文献：
  名称：

  一种在完整糖蛋白上精确化学酶合成 13C 标记的唾液酸寡糖的方法：一种新的单锅 [3-13C]-标记唾液酸类似物的方法，通过控制可逆醛缩酶反应，酶促合成 [3-13C]糖蛋白上的-NeuAc-α-(2→3)-[U-13C]-Gal-β-(1→4)-GlcNAc-β-序列及其构象分析

  摘要：

  A one-pot enzymatic C-13-labeling method for the 3-position of sialic acid (NeuAc) analogues has been developed using NeuAc aldolase, lactate dehydrogenase (LDH), alcohol dehydrogenase (ADI-T), and nucleotide pyrophosphatase (NPP). This method consists of two steps, the first of which is degradation to 2-acetamido-2-deoxy-D-mannose (ManNAc) analogues. This degradation reaction was accelerated by a cofactor regeneration system which converts pyruvic acid into lactic acid using LDH, ADH, and beta-nicotinamide adenine dinucleotide oxidized form (beta-NAD(+)). The second step is condensation of the ManNAc analogue with [3-C-13]-pyruvic acid newly added after decomposition of the cofactor by nucleotide pyrophosphatase which play a role like switch to stop conversion of pyruvic acid into lactic acid. Five different NeuAc analogues have been labeled in good yields using this newly developed one-pot enzymatic procedure. Following conversion of [3-C-13]-NeuAc to CMP-[3-C-13]-NeuAc, enzymatic synthesis of [3-C-13]-NeuAc-alpha-(2-->3)-[U-C-13]-Gal-beta-(1-->4)-GlcNAc-beta-x-ovalbumin (x: hybrid type oligosaccharide) 23 and [3-C-13]-NeuAc-alpha-(2-->3)-[U-C-13]-Gal-beta-(1-->4)-GlcNAc-beta-OMe 26 (sialyl LacNAc) was performed using bovine beta-1,4-galactosyltransferase and rat recombinant alpha-2,3-sialyltransferase. The H-1 chemical shifts of all protons in [3-C-13]-NeuAc-alpha-(2-->3)-[U-C-13]-Gal-beta- on a glycoprotein were assigned by 2D HMQC, 1D HSQC-TOCSY, and the herein described 1D and 2D HSQC-TOCSY-NOESY-TOCSY method. More specifically, the 7-, 8-, and 9-protons of NeuAc could be observed by this HSQC-TOCSY-NOESY-TOCSY method even with only a single C-13 atom at the 3-position. In addition, 1D and 2D HMQC-NOESY spectra as well as carbon spin-lattice relaxation times (T-1) were measured to compare the conformational properties and dynamic behavior of the sialylgalactoside as part of the sialyl LacNAc 26 and when bound to a glycoprotein 23. These analyses suggested that the conformational properties of sialyl LacNAc are similar for both the conjugated and unconjugated forms, and that the torsional angle of the sialyl linkage, i.e., COOH-C2(NeuAc)-O-C3(Gal), is biased toward the anti (-146.7 degrees) conformation. In addition, the flexibility of galactosyl ring when bound to a glycoprotein appears to be significantly restricted by the attachment of NeuAc as compared with unconjugated sialyl LacNAc.

  DOI：

  10.1021/ja994211j