amylostatin XG

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: amylostatin XG
• 英文别名: Amylostatin XG；(3R,4R,5S,6R)-5-[(2R,3R,4S,5S,6R)-3,4-dihydroxy-6-methyl-5-[[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino]oxan-2-yl]oxy-6-(hydroxymethyl)oxane-2,3,4-triol
• 化学式: C₁₉H₃₃NO₁₃
• 分子量: 483.47
• InChiKey: SNMISNLUIRCRQE-YOQJKDJJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.4
• 重原子数：
  33
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  242
• 氢给体数：
  11
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  amylostatin XG 在 sodium tetrahydroborate 作用下， 以 水 为溶剂， 反应 2.0h， 生成 Amylostatin XG_H
  参考文献：
  名称：

  Fukuhara, Ken-ichi; Murai, Hidetsugu; Murao, Sawao, Agricultural and Biological Chemistry, 1982, vol. 46, # 8, p. 2021 - 2030

  摘要：

  DOI：
• 作为产物：
  描述：

  acarbose 在 硫酸 作用下， 反应 2.0h， 以31 g的产率得到amylostatin XG
  参考文献：
  名称：

  抗结构性α-d-葡萄糖苷酶抑制剂阿卡波糖

  摘要：

  摘要肠道α-d-葡萄糖苷酶的有效抑制剂和有效的口服降糖药假四糖阿卡波糖（1）的水解得到d-葡萄糖和三环化合物（1 R，2 S，3 R，4a S，7 R ，8 S，8a S，9a R）-1,2,3,4a，7,8,8a，9a-八氢-1,2,7,8-四羟基-3-[（1 R）-1-羟乙基] -6-羟甲基吡咯并-[2,1-b]苯并恶唑（6）进一步降解为1 l-（1,2,4 / 3）-1-羟甲基-2,3,4-环己三醇（validatol，25 ）和（2 R，3 S，4 S）-2-[（（1 R）-1-羟乙基]-吡咯烷-3,4-二醇（49））的硼氢化钠还原反应，然后进行催化氢化。1的甲醇分解得到α-和β-糖苷11和10，它们通过氢化裂解而得到25和甲基的4-氨基-4,6-二脱氧-α-和β-d-葡萄糖吡喃糖的α-和β-糖苷（紫草胺） ，38）。氢化后，有1个给出了 除了几种次要产品外，还有25和碱性三糖被乙酰化为viosamine

  DOI：

  10.1016/0008-6215(84)85333-1

文献信息

• Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors
  作者：Kwan Hwa Park、Myo Jeong Kim、Hee Seob Lee、Nam Soo Han、Doman Kim、John F Robyt

  DOI：10.1016/s0008-6215(98)00276-6

  日期：1998.12

  products in which PTS was primarily attached alpha-(1-->6) to D-glucose, D-mannose, D-galactose, and methyl alpha-D-glucopyranoside. With D-fructopyranose and D-xylopyranose, PTS was linked alpha-(1-->5) and alpha-(1-->4), respectively. PTS was primarily transferred to C-6 of the nonreducing residue of maltose, cellobiose, lactose, and gentiobiose. Lesser amounts of alpha-(1-->3) and/or alpha-(1-->4) transfer

  观察到，嗜热脂肪芽孢杆菌麦芽糖淀粉酶裂解了阿卡波糖的第一个糖苷键以产生葡萄糖和伪三糖（PTS），该伪三糖被转移到葡萄糖的C-6上形成α-（1-> 6）糖苷键，并且异卡波糖的形成。在消化液中添加许多不同的碳水化合物可得到转移产物，其中PTS主要附着在D-葡萄糖，D-甘露糖，D-半乳糖和甲基α-D-吡喃葡萄糖苷上α-（1-> 6）。用D-果糖吡喃糖和D-木吡喃糖将PTS分别链接为alpha-（1-> 5）和alpha-（1-> 4）。PTS主要转移到麦芽糖，纤维二糖，乳糖和龙胆二糖的非还原性残基的C-6上。这些碳水化合物受体也观察到较少量的α-（1-> 3）和/或α-（1-> 4）转移产物。蔗糖的主要转移产物使PTS连接到葡萄糖残基的alpha-（1-> 4）上。α，α-海藻糖产生了两种主要产品，PTS链接了alpha-（1-> 6）和alpha-（1-> 4）。麦芽糖醇给出了两种主要产物，其
• Morita, Naofumi; Takagi, Masanosuke, Agricultural and Biological Chemistry, 1983, vol. 47, # 9, p. 2111 - 2112
  作者：Morita, Naofumi、Takagi, Masanosuke

  DOI：——

  日期：——
• Enzymatic Synthesis of a Selective Inhibitor for α-Glucosidases: α-Acarviosinyl-(1→9)-3-α-<scp>d</scp>-glucopyranosylpropen
  作者：Young-Su Lee、Myoung-Hee Lee、Hee-Seob Lee、Seung-Jae Lee、Young-Wan Kim、Ran Zhang、Stephen G. Withers、Kwan Soo Kim、Sung-Joon Lee、Kwan-Hwa Park

  DOI：10.1021/jf703655k

  日期：2008.7.1

  Here, we describe the enzymatic synthesis of novel inhibitors using acarviosine-glucose, as a donor and 3-alpha-D-glucopyranosylpropen (alpha GP) as an acceptor. Maltogenic amylase from Thermus sp. (ThMA) catalyzed the transglycosylation of the acarviosine moiety to alpha GP. The two major reaction products were isolated using chromatographies. Structural analyses revealed that acarviosine was transferred to either C-7 or C-9 of the alpha GP, which correspond to C-4 and C-6 of glucose. Both inhibited rat intestine (x-glucosidase competitively but displayed a mixed-type inhibition mode against human pancreatic alpha-amylase. The alpha-acarviosinyl-(1 -> 7)-3-alpha-D-glucopyranosylpropen showed weaker inhibition potency than acarbose against both alpha-glycosidases. In contrast, the alpha-acarviosinyl-(1 -> 9)-3-alpha-D-glucopyranosylpropen exhibited a 3.0-fold improved inhibition potency against rat intestine a-glucosidase with 0.3-fold inhibition potency against human pancreatic a-amylase relative to acarbose. In conclusion, alpha-acarviosinyl-(1 -> 9)-3-alpha-D-glucopyranosylpropen is a novel alpha-glucosidase-selective inhibitor with 10-fold enhanced selectivity toward alpha-glucosidase over alpha-amylase relative to acarbose, and it could be applied as a potent hypoglycemic agent.
• Enzymatic synthesis of a new inhibitor of α-amylases: acarviosinyl-isomaltosyl-spiro-thiohydantoin
  作者：Lili Kandra、Judit Remenyik、Gyula Batta、László Somsák、Gyöngyi Gyémánt、Kwan Hwa Park

  DOI：10.1016/j.carres.2005.03.003

  日期：2005.5

  Synthesis of acarviosinyl-isomaltosyl-spiro-thiohydantoin in yields up to 20%, has been achieved by Bacillus stearothermophilus maltogenic amylase (BSMA). BSMA is capable of transferring the acarviosine-glucose residue from an acarbose donor onto glucopyranosylidene-spiro-thiohydantoin. Reactions were followed using HPLC and MALDI-TOF MS. (1H and 13C NMR studies revealed that the enzyme reserved its stereoselectivity. Glycosylation took place mainly at C-6 resulting in a-acarviosinyl-(14)-a-D-glucopyranosyl-(16)-D-glucopyranosylidene-spiro-thiohydantoin. This compound was found to be a much more efficient salivary amylase inhibitor than glucopyranosylidene-spiro-thiohydantoin with kinetic constants of K)(EI) (= 0.19 mM and K)(ESI) = 0.24 mM. 2005 Elsevier Ltd. All rights reserved.