D-mannopyranosyl

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: D-mannopyranosyl
• 英文别名: O-β-D-mannopyranosyl-(1->2)-D-mannopyranose；β-D-Man p-(1->2)-D-Man；β-D-mannopyranosyl-(1→2)-D-mannopyranose；β-Man-(1→2)-Man；2-O-β-D-Mannopyranosyl-α,β-D-mannose；2-O-beta-D-mannopyranosyl-D-mannopyranose；(3S,4S,5S,6R)-6-(hydroxymethyl)-3-[(2S,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxane-2,4,5-triol
• 化学式: C₁₂H₂₂O₁₁
• 分子量: 342.3
• InChiKey: HIWPGCMGAMJNRG-FZFXURTHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.2
• 重原子数：
  23
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  190
• 氢给体数：
  8
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  D-mannopyranosyl 在 硫酸 作用下， 反应 3.0h， 生成 D-甘露糖
  参考文献：
  名称：

  Iwahara, Shojiro; Tanaka, Tadashi, Agricultural and Biological Chemistry, 1988, vol. 52, # 1, p. 9 - 14

  摘要：

  DOI：
• 作为产物：
  描述：

  β-D-(1,2)-mannotriose 、 水 生成 D-甘露糖 、 D-mannopyranosyl
  参考文献：
  名称：

  The GH130 Family of Mannoside Phosphorylases Contains Glycoside Hydrolases That Target β-1,2-Mannosidic Linkages in Candida Mannan

  摘要：

  The depolymerization of complex glycans is an important biological process that is of considerable interest to environmentally relevant industries. beta-Mannose is a major component of plant structural polysaccharides and eukaryotic N-glycans. These linkages are primarily cleaved by glycoside hydrolases, although recently, a family of glycoside phosphorylases, GH130, have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages. In these phosphorylases, bond cleavage was mediated by a single displacement reaction in which phosphate functions as the catalytic nucleophile. A cohort of GH130 enzymes, however, lack the conserved basic residues that bind the phosphate nucleophile, and it was proposed that these enzymes function as glycoside hydrolases. Here we show that two Bacteroides enzymes, BT3780 and BACOVA_03624, which lack the phosphate binding residues, are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism. Because the genes encoding these enzymes are located in genetic loci that orchestrate the depolymerization of yeast alpha-mannans, it is likely that the two enzymes target the beta-1,2-mannose residues that cap the glycan produced by Candida albicans. The crystal structure of BT3780 in complex with mannose bound in the -1 and +1 subsites showed that a pair of glutamates, Glu(227) and Glu(268), hydrogen bond to O-1 of alpha-mannose, and either of these residues may function as the catalytic base. The candidate catalytic acid and the other residues that interact with the active site mannose are conserved in both GH130 mannoside phosphorylases and beta-1,2-mannosidases. Functional phylogeny identified a conserved lysine, Lys(199) in BT3780, as a key specificity determinant for beta-1,2-mannosidic linkages.

  DOI：

  10.1074/jbc.m115.681460

文献信息

• Synthesis of a biotinylated probe from biotechnologically derived β-d-mannopyranosyl-(1 → 2)-d-mannopyranose for assessment of carbohydrate specificity of antibodies
  作者：Alexander A. Karelin、Nadezhda E. Ustyuzhanina、Yury E. Tsvetkov、Nikolay E. Nifantiev

  DOI：10.1016/j.carres.2018.10.013

  日期：2019.1

  The disaccharide β-d-mannopyranosyl-(1 → 2)-d-mannopyranose obtained by chemical cleavage and enzymatic dephosphorylation of biotechnologically available phosphomannan was transformed over six steps into a biotinylated probe suitable for assessment of carbohydrate specificity of antibodies induced by yeast cell wall preparations.

  通过对生物技术上可利用的磷酸甘露聚糖进行化学裂解和酶促脱磷酸作用而获得的二糖β-d-甘露吡喃糖基-（1→2）-d-甘露吡喃糖经六步转化为生物素化探针，适用于评估酵母细胞壁诱导的抗体的碳水化合物特异性准备。
• Discovery of Two β-1,2-Mannoside Phosphorylases Showing Different Chain-Length Specificities from Thermoanaerobacter sp. X-514
  作者：Kazuhiro Chiku、Takanori Nihira、Erika Suzuki、Mamoru Nishimoto、Motomitsu Kitaoka、Ken'ichi Ohtsubo、Hiroyuki Nakai

  DOI：10.1371/journal.pone.0114882

  日期：——

  We characterized Teth514_1788 and Teth514_1789, belonging to glycoside hydrolase family 130, from Thermoanaerobacter sp. X-514. These two enzymes catalyzed the synthesis of 1,2-β-oligomannan using β-1,2-mannobiose and d-mannose as the optimal acceptors, respectively, in the presence of the donor α-d-mannose 1-phosphate. Kinetic analysis of the phosphorolytic reaction toward 1,2-β-oligomannan revealed that these enzymes followed a typical sequential Bi Bi mechanism. The kinetic parameters of the phosphorolysis of 1,2-β-oligomannan indicate that Teth514_1788 and Teth514_1789 prefer 1,2-β-oligomannans containing a DP ≥3 and β-1,2-Man2, respectively. These results indicate that the two enzymes are novel inverting phosphorylases that exhibit distinct chain-length specificities toward 1,2-β-oligomannan. Here, we propose 1,2-β-oligomannan:phosphate α-d-mannosyltransferase as the systematic name and 1,2-β-oligomannan phosphorylase as the short name for Teth514_1788 and β-1,2-mannobiose:phosphate α-d-mannosyltransferase as the systematic name and β-1,2-mannobiose phosphorylase as the short name for Teth514_1789.

  我们鉴定了来自X-514热厌氧菌的属于糖苷水解酶家族130的Teth514_1788和Teth514_1789。在供体α-d-甘露糖1-磷酸的存在下，这两种酶分别以β-1,2-甘露糖和d-甘露糖作为最佳受体，催化1,2-β-寡甘露聚糖的合成。对1,2-β-寡甘露聚糖的磷解反应的动力学分析表明，这些酶遵循典型的Bi Bi顺序机制。1,2-β-寡甘露聚糖的磷解动力学参数表明，Teth514_1788和Teth514_1789分别偏好DP≥3和β-1,2-Man2的1,2-β-寡甘露聚糖。这些结果表明，这两种酶是新型的逆磷酸化酶，对1,2-β-寡甘露聚糖表现出不同的链长特异性。在此，我们建议将1,2-β-寡甘露聚糖：磷酸α-d-甘露糖转移酶作为系统名称，将1,2-β-寡甘露聚糖磷酸化酶作为Teth514_1788的简称，将β-1,2-甘
• Epimerization of reducing terminal groups of (1 → 2)-linked d-gluco- and d-manno-disaccharides in aqueous sodium hydroxide
  作者：Hidemitsu Kobayashi、Nobuyuki Shibata、Shigeko Konno、Kanehiko Hisamicha、Shigeo Suzuki

  DOI：10.1016/s0008-6215(00)90583-4

  日期：1992.5
• Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from <i>Listeria innocua</i>
  作者：Tomohiro Tsuda、Takanori Nihira、Kazuhiro Chiku、Erika Suzuki、Takatoshi Arakawa、Mamoru Nishimoto、Motomitsu Kitaoka、Hiroyuki Nakai、Shinya Fushinobu

  DOI：10.1016/j.febslet.2015.11.034

  日期：2015.12.21

  Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for β‐mannosides. Here, we characterized β‐1,2‐mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with β‐1,2‐linked mannooligosaccharides. β‐1,2‐Mannotriose was bound in a U‐shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant open–close loop displacement was observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis was provided.
• An inverting β-1,2-mannosidase belonging to glycoside hydrolase family 130 from<i>Dyadobacter fermentans</i>
  作者：Takanori Nihira、Kazuhiro Chiku、Erika Suzuki、Mamoru Nishimoto、Shinya Fushinobu、Motomitsu Kitaoka、Ken'ichi Ohtsubo、Hiroyuki Nakai

  DOI：10.1016/j.febslet.2015.10.008

  日期：2015.11.30

  The glycoside hydrolase family (GH) 130 is composed of inverting phosphorylases that catalyze reversible phosphorolysis of β‐d‐mannosides. Here we report a glycoside hydrolase as a new member of GH130. Dfer_3176 from Dyadobacter fermentans showed no synthetic activity using α‐d‐mannose 1‐phosphate but it released α‐d‐mannose from β‐1,2‐mannooligosaccharides with an inversion of the anomeric configuration, indicating that Dfer_3176 is a β‐1,2‐mannosidase. Mutational analysis indicated that two glutamic acid residues are critical for the hydrolysis of β‐1,2‐mannotriose. The two residues are not conserved among GH130 phosphorylases and are predicted to assist the nucleophilic attack of a water molecule in the hydrolysis of the β‐d‐mannosidic bond.