3-O-β-D-glucopyranosyl-D-mannose | 37085-18-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 3-O-β-D-glucopyranosyl-D-mannose
• 英文别名: Glc(b1-3)aldehydo-Man；(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-[(2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyhexanal
• CAS: 37085-18-0
• 化学式: C₁₂H₂₂O₁₁
• 分子量: 342.3
• InChiKey: YGEHCIVVZVBCLE-VOXHDCLVSA-N

物化性质

• 沸点：
  790.1±60.0 °C(Predicted)
• 密度：
  1.68±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -5
• 重原子数：
  23
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  197
• 氢给体数：
  8
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  昆布六糖 在 3-吗啉丙磺酸 、 Paenibacillus sp. YM-1 laminaribiose phosphorylase 、 磷酸肌酸 、 sodium hydroxide 作用下， 以 水 为溶剂， 反应 0.17h， 生成 3-O-β-D-glucopyranosyl-D-mannose
  参考文献：
  名称：

  Characterization of a Bacterial Laminaribiose Phosphorylase

  摘要：

  细菌片状木糖磷酸化酶（LBPbac）是首次从无细胞提取物中发现并纯化的。它能将层压木糖磷酸化成 1-磷酸α-葡萄糖和葡萄糖，但不能磷酸化其他葡萄糖。它能轻微地磷酸化层状三糖和更高的层状寡糖。底物聚合度的特异性明显不同于鳗鲡酶（LBPEug）：与 LBPEug 相比，LBPbac 对层压木糖的特异性更高。它在反向磷酸化过程中表现出与 LBPEug 相似的受体特异性。克隆 LBPbac（lbpA）的编码基因发现，LBPbac 是葡萄糖苷水解酶 94 家族的成员，该家族包括纤维生物糖磷酸化酶、纤维糊精磷酸化酶和 N,N′-二乙酰壳寡糖磷酸化酶。在 lbpA 的上游发现了编码专门针对片状寡糖的 ATP 结合盒糖转运体成分的基因，这表明 LBPbac 的作用是利用细胞外产生的片状木糖。这种作用与 LBPEug 的作用不同，后者参与利用细胞内储存的 1,3-β 葡聚糖--帕拉米隆。

  DOI：

  10.1271/bbb.110772

文献信息

• Processes and host cells for genome, pathway, and biomolecular engineering
  申请人：enEvolv, Inc.

  公开号：US10370654B2

  公开（公告）日：2019-08-06

  The present disclosure provides compositions and methods for genomic engineering.

  本公开提供了基因组工程的组合物和方法。
• Characterization of a laminaribiose phosphorylase from Acholeplasma laidlawii PG-8A and production of 1,3-β-d-glucosyl disaccharides
  作者：Takanori Nihira、Yuka Saito、Motomitsu Kitaoka、Mamoru Nishimoto、Ken’ichi Otsubo、Hiroyuki Nakai

  DOI：10.1016/j.carres.2012.08.006

  日期：2012.11

  We identified a glycoside hydrolase family 94 homolog (ACL0729) from Acholeplasma laidlawii PG-8A as a laminaribiose (1,3-beta-D-glucobiose) phosphorylase (EC 2.4.1.31). The recombinant ACL0729 produced in Escherichia coli catalyzed phosphorolysis of laminaribiose with inversion of the anomeric configuration in a typical sequential bi bi mechanism releasing alpha-D-glucose 1-phosphate and D-glucose. Laminaritriose (1,3-beta-D-glucotriose) was not an efficient substrate for ACL0729. The phosphorolysis is reversible, enabling synthesis of 1,3-beta-D-glucosyl disaccharides by reverse phosphorolysis with strict regioselectivity from alpha-D-glucose 1-phosphate as the donor and suitable monosaccharide acceptors (D-glucose, 2-deoxy-D-arabino-hexopyranose, D-xylose, D-glucuronic acid, 1,5-anhydro-D-glucitol, and D-mannose) with C-3 and C-4 equatorial hydroxyl groups. The D-glucose and 2-deoxy-D-arabino-hexopyranose caused significantly strong competitive substrate inhibition compared with other glucobiose phosphorylases reported, in which the acceptor competitively inhibited the binding of the donor substrate. By contrast, none of the examined disaccharides served as acceptor in the synthetic reaction. (C) 2012 Elsevier Ltd. All rights reserved.
• PROCESSES AND HOST CELLS FOR GENOME, PATHWAY, AND BIOMOLECULAR ENGINEERING
  申请人：ENEVOLV, INC.

  公开号：US20160186168A1

  公开（公告）日：2016-06-30

  The present disclosure provides compositions and methods for genomic engineering.
• US9944925B2
  申请人：——

  公开号：US9944925B2

  公开（公告）日：2018-04-17
• Characterization of a Bacterial Laminaribiose Phosphorylase
  作者：Motomitsu KITAOKA、Yasuyuki MATSUOKA、Kiyotaka MORI、Mamoru NISHIMOTO、Kiyoshi HAYASHI

  DOI：10.1271/bbb.110772

  日期：2012.2.23

  Bacterial laminaribiose phosphorylase (LBPbac) was first identified and purified from cell-free extract of Paenibacillus sp. YM-1. It phosphorolyzed laminaribiose into α-glucose 1-phosphate and glucose, but did not phosphorolyze other glucobioses. It slightly phosphorolyzed laminaritriose and higher laminarioligosaccharides. The specificity of the degree of polymerization of the substrate was clearly different from that of the enzyme of Euglena gracilis (LBPEug): LBPbac was more specific to laminaribiose than LBPEug. It showed acceptor specificity in reverse phosphorolysis similar to LBPEug. Cloning of the gene encoding LBPbac (lbpA) has revealed that LBPbac is a member of the glucoside hydrolase family 94, which includes cellobiose phosphorylase, cellodextrin phosphorylase, and N,N′-diacetylchitobiose phosphorylase. The genes that encode the components of an ATP-binding cassette sugar transporter specific to laminarioligosaccharides were identified upstream of lbpA, suggesting that the role of LBPbac is to utilize laminaribiose generated outside the cell. This role is different from that of LBPEug, which participates in the utilization of paramylon, the intracellular storage 1,3-β-glucan.

  细菌片状木糖磷酸化酶（LBPbac）是首次从无细胞提取物中发现并纯化的。它能将层压木糖磷酸化成 1-磷酸α-葡萄糖和葡萄糖，但不能磷酸化其他葡萄糖。它能轻微地磷酸化层状三糖和更高的层状寡糖。底物聚合度的特异性明显不同于鳗鲡酶（LBPEug）：与 LBPEug 相比，LBPbac 对层压木糖的特异性更高。它在反向磷酸化过程中表现出与 LBPEug 相似的受体特异性。克隆 LBPbac（lbpA）的编码基因发现，LBPbac 是葡萄糖苷水解酶 94 家族的成员，该家族包括纤维生物糖磷酸化酶、纤维糊精磷酸化酶和 N,N′-二乙酰壳寡糖磷酸化酶。在 lbpA 的上游发现了编码专门针对片状寡糖的 ATP 结合盒糖转运体成分的基因，这表明 LBPbac 的作用是利用细胞外产生的片状木糖。这种作用与 LBPEug 的作用不同，后者参与利用细胞内储存的 1,3-β 葡聚糖--帕拉米隆。