alpha-Neu5Ac-(2->3)-beta-Gal-(1->3)-beta-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-Gal-(1->4)-beta-Glc-(1<->1')-Cer(d18:1/18:0)(2-)

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 鞘脂
• 英文名称: alpha-Neu5Ac-(2->3)-beta-Gal-(1->3)-beta-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-Gal-(1->4)-beta-Glc-(1<->1')-Cer(d18:1/18:0)(2-)
• 英文别名: (2S,4S,5R,6R)-5-acetamido-2-[(2R,3R,4S,5S,6R)-2-[(2S,3R,4R,5R,6R)-3-acetamido-2-[(2R,3S,4R,5R,6S)-4-[(2S,4S,5R,6R)-5-acetamido-2-carboxylato-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxan-2-yl]oxy-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(E,2S,3R)-3-hydroxy-2-(octadecanoylamino)octadec-4-enoxy]oxan-3-yl]oxy-5-hydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-4-hydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylate
• 化学式: C84H146N4O39-2
• 分子量: 1836.1
• InChiKey: RXIWRIRPTSKUTD-BFJDPXHSSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  127
• 可旋转键数：
  57
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  692
• 氢给体数：
  23
• 氢受体数：
  39

反应信息

• 作为产物：
  描述：

  cytidine monophospho-N-acetylneuraminic acid 、 ganglioside GM1(1-) 生成 cytidine 5'-monophosphate 、 alpha-Neu5Ac-(2->3)-beta-Gal-(1->3)-beta-GalNAc-(1->4)-[alpha-Neu5Ac-(2->3)]-beta-Gal-(1->4)-beta-Glc-(1<->1')-Cer(d18:1/18:0)(2-) 、 氢(+1)阳离子
  参考文献：
  名称：

  人Gal Gal 1,3GalNAc alpha 2,3-唾液酸转移酶（hST3Gal II）的分子克隆和表达。

  摘要：

  从人肝脏cDNA文库中分离出人Gal Gal 1,3GalNAcα2,3-唾液酸转移酶（hST3Gal II）的cDNA，该糖对糖脂的受体底物偏好性比糖蛋白的O-连接寡糖高得多。使用先前克隆的小鼠ST3Gal II（mST3Gal II）cDNA作为探针进行噬菌斑杂交。该cDNA与mST3Gal II的比较分析表明，在预测的编码区中两个序列之间的核苷酸和氨基酸水平分别同源性为89％和94％。Northern分析表明，hST3Gal II mRNA的表达是组织特异性的，在骨骼肌和心脏中很明显，而在肺和肾脏中很低。在COS细胞中表达的这种酶显示出与mST3Gal II相似的活性。

  DOI：

  10.1006/bbrc.1996.1660

文献信息

• Molecular cloning and expression of Galbeta1,3GalNAcalpha2,3-sialyltransferase from mouse brain
  作者：Young-Choon LEE、Nobuyuki KUROSAWA、Toshiro HAMAMOTO、Takashi NAKAOKA、Shuichi TSUJI

  DOI：10.1111/j.1432-1033.1993.tb18155.x

  日期：1993.9

  DNA clones encoding β‐galactoside α2,3‐sialyltransferase have been isolated from mouse brain cDNA libraries using sequence information obtained from the conserved amino acid sequence of the previously cloned enzymes. The cDNA sequence revealed an open reading frame coding for 337 amino acids, and the deduced amono acid sequence showed 80% identity with that of porcine submaxillary gland Galβ1,3GalNAc α2,3‐sialyltransferase. The primary structure of this enzyme suggested a putative domain structure, like that in other glycosyltransferases, consisting of a short NH2‐terminal cytoplasmic domain, a signal‐membrane anchor domain, a proteolytically sensitive stem region, and a large COOH‐terminal active domain. The identity of this enzyme was confirmed by construction of a recombinant sialyltransferase in which the NH2‐terminal part including the cytoplasmic tail, signal‐anchor domain and stem region was replaced with an immuno‐globulin signal sequence. The expression of this recombinant in COS‐7 cells resulted in secretion of a catalytically active and soluble form of the enzyme into the medium. This enzyme exhibited the transferase activity toward only the disaccharide moiety of Galβ1,3GalNAc of glycoproteins and glycolipids, no significant activity being detected for the other substrates tested.
• Kinetic Properties and Acceptor Substrate Preferences of Two Kinds of Gal.beta.1,3GalNAc .alpha.2,3-Sialyltransferase from Mouse Brain
  作者：Naoya Kojima、Young-Choon Lee、Toshiro Hamamoto、Nobuyuki Kurosawa、Shuichi Tsuji

  DOI：10.1021/bi00185a014

  日期：1994.5.17

  The cDNAs encoding two kinds of Gal beta 1,3GalNAc alpha 2,3-sialyltransferases (ST3GalA.1 and ST3GalA.2) have been cloned from mouse brain, both of which could synthesize the NeuAc alpha 2,3Gal beta 1,3GalNAc sequence of gangliosides as well as O-glycosidically linked oligosaccharides of glycoproteins [Lee et al. (1993) Eur. J. Biochem. 216, 377-385; Lee et al. (1994) J. Biol. Chem. (in press)]. Kinetic analysis of the two sialyltransferases using Gal beta 1,3GalNAc, asialoGM1, or asialofetuin revealed that ST3GalA.1 exhibits the highest K-m value for asialoGM1 (K-m = 1.25 mM) and the lowest one for asialofetuin (K-m = 0.10 mM), whereas the K-m values of ST3GalA.2 for the substrates are very similar (K-m approximate to 0.5 mM). The synthesis of GM Ib from asialoGM1 by ST3GalA.1 was clearly inhibited in the presence of Gal beta 1,3GalNAc or asialofetuin, but that by ST3GalA.2 was not at all. On the other hand, the activity of ST3GalA.2 toward Gal beta 1,3GalNAc or asialofetuin was inhibited by asialoGM1 or GM1. The results of acceptor competition experiments involving asialoGM1, Gal beta 1,3GalNAc, and asialofetuin indicated that ST3GalA.2 exhibits noncompetitive inhibition between asialoGM1 and Gal beta 1,3GalNAc or between asialoGM1 and asialofetuin, whereas ST3GalA.1 exhibits competitive inhibition between all kinds of accepters. These results strongly indicate that acceptor preference of ST3GalA.1 is different from that of ST3GalA.2, although their acceptor substrate specificities are the same; i.e., gangliosides serve as predominant accepters for the latter over O-glycosidically linked oligosaccharides of glycoproteins, which are much better accepters for the former.
• Kitagawa H.; Paulson J.C., J Biol Chem, 1994, 0021-9258, 1394-401
  作者：Kitagawa H.、Paulson J.C.

  DOI：——

  日期：——
• Lee Y.-C.; Kojima N.; Wada E., J Biol Chem, 1994, 0021-9258, 10028-33
  作者：Lee Y.-C.、Kojima N.、Wada E.、Kurosawa N.、Nakaoka T.、Hamamoto T.、Tsuji S.

  DOI：——

  日期：——