[(3S,4S,5S,6R)-3-[[(2R,3S,4S,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-methyloxan-3-yl]amino]-4,5,6-trihydroxycyclohexen-1-yl]methyl hydrogen phosphate

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: [(3S,4S,5S,6R)-3-[[(2R,3S,4S,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-methyloxan-3-yl]amino]-4,5,6-trihydroxycyclohexen-1-yl]methyl hydrogen phosphate
• 化学式: C25H43NO21P-
• 分子量: 724.6
• InChiKey: VXXDSQWLTKKGLO-UGEKTDRHSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -12.6
• 重原子数：
  48
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.92
• 拓扑面积：
  378
• 氢给体数：
  13
• 氢受体数：
  21

反应信息

• 作为产物：
  描述：

  Acarbose(1+) 、 adenosine 5'-triphosphate 生成 [(3S,4S,5S,6R)-3-[[(2R,3S,4S,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,3S,4R,5R)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-methyloxan-3-yl]amino]-4,5,6-trihydroxycyclohexen-1-yl]methyl hydrogen phosphate 、 adenosine 5'-diphosphate 、 氢(+1)阳离子
  参考文献：
  名称：

  Formation of Acarbose Phosphate by a Cell-free Extract from the Acarbose Producer Actinoplanes sp.

  摘要：

  α-葡萄糖苷酶抑制剂阿卡波糖在与产毒霉菌株的无细胞提取物孵育期间发生改变。该产物的形成取决于ATP的存在。纯化转化产物的色谱和化学性质表明存在磷酸酯。通过核磁共振分析推断出其结构，并显示为阿卡波糖7-磷酸酯。

  DOI：

  10.7164/antibiotics.49.661

文献信息

• Acarbose 7-Phosphotransferase from Actinoplanes sp.: Purification, Properties, and Possible Physiological Function.
  作者：ANNE DREPPER、HERMANN PAPE

  DOI：10.7164/antibiotics.49.664

  日期：——

  A phosphotransferase which modifies the α-glucosidase inhibitor acarbose by phosphorylation at its 7-position was isolated from the acarbose producer Actinoplanes sp. and purified to homogeneity. The sequence of the first 20 amino acids of the enzyme was determined. The enzyme is an ATP-dependent kinase and shows high specificity for acarbose and some related compounds containing the pseudodisaccharide moiety (acarviosin). The product formed by the enzyme, acarbose-7-phosphate, shows a significant lower inhibitory activity towards disaccharidases than acarbose itself. The acarbose producing organism contains a maltase which is inhibited by acarbose, but to a much lesser extent by acarbose-7-phosphate. The possible role of acarbose 7-phosphotransferase as part of a self-defense mechanism against acarbose in the producing organism is discussed.

  从阿卡波糖生产者放线菌（Actinoplanes sp.）中分离并纯化了一种磷酸转移酶，该酶通过在α-葡萄糖苷酶抑制剂阿卡波糖的7位上发生磷酸化作用来改变阿卡波糖。确定了该酶前 20 个氨基酸的序列。该酶是一种 ATP 依赖性激酶，对阿卡波糖和一些含有假二糖分子（阿卡维糖）的相关化合物具有高度特异性。该酶形成的产物--阿卡波糖-7-磷酸对二糖酶的抑制活性明显低于阿卡波糖本身。产生阿卡波糖的生物体含有一种麦芽糖酶，这种酶对阿卡波糖有抑制作用，但对阿卡波糖-7-磷酸的抑制作用要小得多。本文讨论了阿卡波糖-7-磷酸转移酶作为生产阿卡波糖的生物体内自我防御机制的一部分可能发挥的作用。
• Biosynthesis of the C7-cyclitol Moiety of Acarbose inActinoplanes Species SE50/110
  作者：Chang-Sheng Zhang、Ansgar Stratmann、Oliver Block、Ralph Brückner、Michael Podeschwa、Hans-Josef Altenbach、Udo F. Wehmeier、Wolfgang Piepersberg

  DOI：10.1074/jbc.m202375200

  日期：2002.6

  We have previously demonstrated that the biosynthesis of the C-7-cyclitol, called valienol (or valienamine), of the a-glucosidase inhibitor acarbose starts from the cyclization of sedo-heptulose 7-phosphate to 2-epi-5-epivaliolone (Stratmann, A., Mahmud, T., Lee, S., Distler, J., Floss, H. G., and Piepersberg, W. (1999) J. Biol. Chem. 274, 10889-10896). Synthesis of the intermediate 2-epi-5-epi-valiolone is catalyzed by the cyclase AcbC encoded in the biosynthetic (acb) gene cluster of Actinoplanes sp. SE50/110. The acbC gene lies in a possible transcription unit, acbKLMNOC, cluster encompassing putative biosynthetic genes for cyclitol conversion. All genes were heterologously expressed in strains of Streptomyces lividans 66 strains 1326, TK23, and TK64. The AcbK protein was identified as the acarbose 7-kinase, which had been described earlier (Drepper, A., and Pape, H. (1996) J. Antibiot. (Tokyo) 49, 664-668). The multistep conversion of 2-epi-5-epi-valiolone to the final cyclitol moiety was studied by testing enzymatic mechanisms such as dehydration, reduction, epimerization, and phosphorylation. Thus, a phosphotransferase activity was identified modifying 2-epi-5-epi-valiolone by ATP-dependent phosphorylation. This activity could be attributed to the AcbM protein by verifying this activity in S. lividans strain TK64/pCW4123M, expressing His-tagged AcbM. The His-tagged AcbM protein was purified and subsequently characterized as a 2-epi-5-epi-valiolone 7-kinase, presumably catalyzing the first enzyme reaction in the biosynthetic route, leading to an activated form of the intermediate 1-epi-valienol. The AcbK protein could not catalyze the same reaction nor convert any of the other C-7-cyclitol monomers tested. The 2-epi-5-epi-valiolone 7-phosphate was further converted by the AcbO protein to another isomeric and phosphorylated intermediate, which was likely to be the 2-epimer 5-epi-valiolone 7-phosphate. The products of both enzyme reactions were characterized by mass spectrometric methods. The product of the AcbM-catalyzed reaction, 2-epi-5-epi-valiolone 7-phosphate, was purified on a preparative scale and identified by NAIR spectroscopy. A biosynthetic pathway for the pseudodisaccharidic acarviosyl moiety of acarbose is proposed on the basis of these data.
• Formation of Acarbose Phosphate by a Cell-free Extract from the Acarbose Producer Actinoplanes sp.
  作者：KLAUS GOEKE、ANNE DREPPER、HERMANN PAPE

  DOI：10.7164/antibiotics.49.661

  日期：——

  The α-glucosidase inhibitor acarbose is modified during incubation with cell-free extract from the producing Actinoplanes strain. The formation of this product depends on the presence of ATP. Chromatographic and chemical properties of the purified transformation product indicate the presence of a phosphate ester. The structure is deduced by NMR analysis and shown to be acarbose7-phosphate.

  α-葡萄糖苷酶抑制剂阿卡波糖在与产毒霉菌株的无细胞提取物孵育期间发生改变。该产物的形成取决于ATP的存在。纯化转化产物的色谱和化学性质表明存在磷酸酯。通过核磁共振分析推断出其结构，并显示为阿卡波糖7-磷酸酯。