3'-<(3,4,6-tri-O-acetyl-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl)oxy>-6'-hydroxyspiroxanthen>-3-one | 148806-89-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3'-<(3,4,6-tri-O-acetyl-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl)oxy>-6'-hydroxyspiroxanthen>-3-one
• 英文别名: 3'-[[3,4,6-tri-O-acetyl-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]oxy]-6'-hydroxyspiro[isobenzofuran-1(3H),9'-[9H]-xanthen]-3-one；3'-{[3,4,6-tri-O-acetyl-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]oxy}-6'-hydroxyspiro(isobenzofuran-1(3H),9'-[9H]xanthen)-3-one；[(2R,3S,4R,5R,6S)-5-acetamido-3,4-diacetyloxy-6-(6'-hydroxy-3-oxospiro[2-benzofuran-1,9'-xanthene]-3'-yl)oxyoxan-2-yl]methyl acetate
• CAS: 148806-89-7
• 化学式: C₃₄H₃₁NO₁₃
• 分子量: 661.619
• InChiKey: UYMNEUUBLFBPOF-MCTIHYOQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  48
• 可旋转键数：
  10
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  182
• 氢给体数：
  2
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  3'-<(3,4,6-tri-O-acetyl-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl)oxy>-6'-hydroxyspiroxanthen>-3-one 在 sodium methylate 作用下， 以 甲醇 为溶剂， 反应 0.5h， 以70.6%的产率得到3'-<<2-(acetylamino)-2-deoxy-β-D-glucopyranosyl>oxy>-6'-hydroxyspiroxanthen>-3-one
  参考文献：
  名称：

  Glycosides Having Chromophores as Substrates for Sensitive Enzyme Analysis. IV. Synthesis of N-Acetyl-.BETA.-D-glucosaminides of Fluorescein Derivatives and Their Application to the Rate-Assay of N-Acetyl-.BETA.-D-glucosaminidase.

  摘要：

  通过引入 N-乙酰基-β-D-氨基葡萄糖苷，合成了三种新型 N-乙酰基-β-D-氨基葡萄糖苷，即 2'，7'-二氯荧光素单(N-乙酰基-β-D-氨基葡萄糖苷)(6a)、荧光素单(N-乙酰基-β-D-氨基葡萄糖苷)(6b)和 2'、7'-dichlorofluorescein di(N-acetyl-β-D-glucosaminide) (7a)是通过在荧光素衍生物中引入 N-acetyl-β-D-glucosaminyl 基团，然后去除保护基团而合成的。化合物 6a、6b 和 7a 经 N-乙酰基-β-D-葡糖胺苷酶水解后，在弱酸性速率测定条件（pH 值为 5.0）下，产物在长吸收波长（500、465 和 485 纳米）处显示出较高的吸光度。6a 和 7a 的 Km 值分别为 0.56 和 0.86 mM。在这些化合物中，7a 被认为是最有可能用于 N-乙酰基-β-D-葡糖胺酶速率测定的发色底物，因为它在酶水解作用下会产生从无色到橙色的明显颜色变化（λmax 280→485 nm），并且具有超过 30 mM 的较高水溶性。

  DOI：

  10.1248/cpb.41.314
• 作为产物：
  描述：

  荧光素 、 2-乙酰氨基-3,4,6-三-O-乙酰-2-脱氧-α-D-吡喃葡萄糖酰基氯 在 吡啶 、 silver(l) oxide 作用下， 以 乙腈 为溶剂， 反应 48.0h， 以60%的产率得到3'-<(3,4,6-tri-O-acetyl-2-(acetylamino)-2-deoxy-β-D-glucopyranosyl)oxy>-6'-hydroxyspiroxanthen>-3-one
  参考文献：
  名称：

  Enzymatic characterization of O-GlcNAcase isoforms using a fluorogenic GlcNAc substrate

  摘要：

  A highly sensitive fluorogenic hexosaminidase substrate, fluorescein di(N-acetyl-beta-D-glucosaminide) (FDGlcNAc) was prepared essentially as described previously [Chem. Pharm. Bull. 1993, 41, 314] with some modifications. The fluorescent analog is a substrate for a number of hexosaminidases but here we have focused on the cytoplasmic O-GlcNAcase isoforms. Kinetic analysis using purified O-GlcNAcase and its splice variant (v-O-GlcNAcase) expressed in Escherichia coli suggests that FDGlcNAc is a much more efficient substrate (K-m = 84.9 mu M) than the conventional substrate, para-nitrophenyl 2-acetamido-2-deoxy-beta-D-glucopyranoside (pNP-beta-GlcNAc, K-m = 1.1 nM) and a previously developed fluorogenic substrate, 4-methylumbelliferyl 2-acetamido-2-deoxy-beta -D-glucopyranoside [MUGlcNAc, K-m = 0.43 mM; J. Biol. Chem. 2005, 280, 25313] for O-GlcNAcase. The variant O-GlcNAcase. a protein lacking the C-terminal third of the full-length O-GlcNAcase, exhibited a K-m of 2.1 mM with respect to FDGlcNAc. This shorter isoforni was not previously thought to exhibit O-GlcNAcase activity based on in vitro Studies with pNP-beta-GlcNAc. However, both O-GlcNAcase isoforms reduced O-GlcNAc protein levels extracted from HeLa and HT-29 cells in vitro. indicating that the splice variant is a bona fide O-GlcNAcase. Fluorescein di-N-acetyl-beta-D-galactosaminide (FDGalNAc) is not cleaved by these enzymes, consistent with previous findings that the O-GlcNAcase has substrate specificity toward O-GlcNAc but not O-GalNAc. The enzymatic activity of the shorter isoforni of O-GlcNAcase was first detected by using highly sensitive fluorogenic FDGlcNAc substrate. The finding that O-GlcNAcase exists as two distinct isoforms has a number of important implications for the role of O-GlcNAcase in hexosamine signaling. Published by Elsevier Ltd.

  DOI：

  10.1016/j.carres.2006.03.004