3',6'-bis[[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]oxy]-spiro[isobenzofuran-1(3H),9'-[9H]-xanthen]-3-one | 885330-92-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 3',6'-bis[[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]oxy]-spiro[isobenzofuran-1(3H),9'-[9H]-xanthen]-3-one
• 英文别名: N-[(2S,3R,4R,5S,6R)-2-[6'-[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3-oxospiro[2-benzofuran-1,9'-xanthene]-3'-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide
• CAS: 885330-92-7
• 化学式: C₃₆H₃₈N₂O₁₅
• 分子量: 738.702
• InChiKey: VBJMVLGTDHSGMC-HBFLWAKESA-N

物化性质

• 沸点：
  1125.5±65.0 °C(Predicted)
• 密度：
  1.62±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  53
• 可旋转键数：
  8
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  252
• 氢给体数：
  8
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  3',6'-bis[[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]oxy]-spiro[isobenzofuran-1(3H),9'-[9H]-xanthen]-3-one 在 phosphate buffer 、 protein O-GlcNAcase 、 2-羟基丙烷-1,2,3-三羧酸根 作用下， 生成 D-GlcNAc 、 荧光素
  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
• 作为产物：
  描述：

  荧光素 在 吡啶 、 ammonium hydroxide 、 silver(l) oxide 作用下， 以 甲醇 、 乙腈 为溶剂， 反应 51.0h， 生成 3',6'-bis[[2-(acetylamino)-2-deoxy-β-D-glucopyranosyl]oxy]-spiro[isobenzofuran-1(3H),9'-[9H]-xanthen]-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