(2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexanone | 890653-91-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexanone
• 英文别名: 3-amino-2,3-dideoxy-scyllo-inosose；(2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexan-1-one
• CAS: 890653-91-5
• 化学式: C₆H₁₁NO₄
• 分子量: 161.158
• InChiKey: FSUGCKMUTGKWIE-YGIVHSIPSA-N

物化性质

• 沸点：
  341.3±42.0 °C(Predicted)
• 密度：
  1.588±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3
• 重原子数：
  11
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  104
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexanone 在 硼氘化钠 作用下， 反应 1.0h， 生成 [3-2H]-2-deoxy-scyllo-inosamine
  参考文献：
  名称：

  Butirosin生物合成中自由基SAM脱氢酶的表征和机理研究

  摘要：

  在butirosin 生物合成基因簇中编码的BtrN 具有在自由基S-腺苷甲硫氨酸(SAM) 超家族中保守的CXXXCXXC 基序。其在butirosin 生产者环状芽孢杆菌中的基因破坏导致2-脱氧青蟹肌胺(DOIA) 和2-脱氧链霉胺(DOS) 之间的生物合成途径中断。此外，过表达酶的体外测定表明，BtrN 在严格厌氧条件下催化 DOIA 的氧化，同时消耗等摩尔量的 SAM 以产生 5'-脱氧腺苷、甲硫氨酸和 3-氨基-2,3-双脱氧-青蟹肌糖（氨基-DOI）。动力学分析显示底物被 DOIA 抑制，但不被 SAM 抑制，这表明反应是有序 Bi Ter 机制，SAM 是第一个底物，DOIA 是第二个底物。BtrN 与 [3-2 H] DOIA 反应生成非标记、单氘和双氘 5'-脱氧腺苷，而未通过在氧化氘缓冲液中孵育非标记 DOIA 而掺入氘。这些结果表明，DOIA 的 C-3 处的氢原子直接转移到

  DOI：

  10.1021/ja072481t
• 作为产物：
  描述：

  2-deoxystreptamine 在 BtrS 磷酸吡哆醛 、 丙酮酸 作用下， 反应 3.0h， 生成 (2R,3S,4R,5S)-5-amino-2,3,4-trihydroxycyclohexanone
  参考文献：
  名称：

  Butirosin生物合成中自由基SAM脱氢酶的表征和机理研究

  摘要：

  在butirosin 生物合成基因簇中编码的BtrN 具有在自由基S-腺苷甲硫氨酸(SAM) 超家族中保守的CXXXCXXC 基序。其在butirosin 生产者环状芽孢杆菌中的基因破坏导致2-脱氧青蟹肌胺(DOIA) 和2-脱氧链霉胺(DOS) 之间的生物合成途径中断。此外，过表达酶的体外测定表明，BtrN 在严格厌氧条件下催化 DOIA 的氧化，同时消耗等摩尔量的 SAM 以产生 5'-脱氧腺苷、甲硫氨酸和 3-氨基-2,3-双脱氧-青蟹肌糖（氨基-DOI）。动力学分析显示底物被 DOIA 抑制，但不被 SAM 抑制，这表明反应是有序 Bi Ter 机制，SAM 是第一个底物，DOIA 是第二个底物。BtrN 与 [3-2 H] DOIA 反应生成非标记、单氘和双氘 5'-脱氧腺苷，而未通过在氧化氘缓冲液中孵育非标记 DOIA 而掺入氘。这些结果表明，DOIA 的 C-3 处的氢原子直接转移到

  DOI：

  10.1021/ja072481t

文献信息

• Stereochemical Recognition of Doubly Functional Aminotransferase in 2-Deoxystreptamine Biosynthesis
  作者：Kenichi Yokoyama、Fumitaka Kudo、Mieko Kuwahara、Kousuke Inomata、Hideyuki Tamegai、Tadashi Eguchi、Katsumi Kakinuma

  DOI：10.1021/ja0445948

  日期：2005.4.1

  The doubly functional aminotransferase BtrS in the 2-deoxystreptamine (DOS) biosynthesis, in which two transaminations are involved, was characterized by a genetic as well as a chemical approach with the heterologously expressed enzyme. The gene disruption study clearly showed that BtrS is involved, in addition to the previously confirmed first transamination, in the second transamination as well. This dual function of BtrS for the DOS biosynthesis was further confirmed by the structural determination of the reverse reaction product from DOS. Enantiospecific formation of the reverse reaction product from DOS clearly showed that BtrS distinguishes the enantiotopic amino groups of DOS, but in contrast, both enantiomers of 2-deoxy-scyllo-inosose (DOI) were efficiently accepted by BtrS to give a racemic product. This unique stereochemical recognition of DOI chirality and DOS prochirality by BtrS is mechanistically explained by a specific hydrogen-bond donating force in the enzyme active site as a particular feature of this doubly functional enzyme.
• Electrochemical Resolution of the [4Fe-4S] Centers of the AdoMet Radical Enzyme BtrN: Evidence of Proton Coupling and an Unusual, Low-Potential Auxiliary Cluster
  作者：Stephanie J. Maiocco、Tyler L. Grove、Squire J. Booker、Sean J. Elliott

  DOI：10.1021/jacs.5b03384

  日期：2015.7.15

  The S-adenosylmethionine (AdoMet) radical superfamily of enzymes includes over 113 500 unique members, each of which contains one indispensable iron-sulfur (FeS) cluster that is required to generate a 5'-deoxyadenosyl 5'-radical intermediate during catalysis. Enzymes within several subgroups of the superfamily, however, have been found to contain one or more additional FeS clusters. While these additional clusters are absolutely essential for enzyme activity, their exact roles in the function and/or mechanism of action of many of the enzymes are at best speculative, indicating a need to develop methods to characterize and study these clusters in more detail. Here, BtrN, an AdoMet radical dehydrogenase that catalyzes the two-electron oxidation of 2-deoxy-scyllo-inosamine to amino-dideoxy-scyllo-inosose, an intermediate in the biosynthesis of 2-deoxystreptamine antibiotics, is examined through direct electrochemistry, where the potential of both its AdoMet radical and auxiliary [4Fe-4S] clusters can be measured simultaneously. We find that the AdoMet radical cluster exhibits a midpoint potential of -510 mV, while the auxiliary cluster exhibits a midpoint potential of -765 mV, to our knowledge the lowest [4Fe-4S](2+/+) potential to be determined to date. The impact of AdoMet binding and the pH dependence of catalysis are also quantitatively observed. These data show that direct electrochemical methods can be used to further elucidate the chemistry of the burgeoning AdoMet radical superfamily in the future.
• A Consensus Mechanism for Radical SAM-Dependent Dehydrogenation? BtrN Contains Two [4Fe-4S] Clusters
  作者：Tyler L. Grove、Jessica H. Ahlum、Priya Sharma、Carsten Krebs、Squire J. Booker

  DOI：10.1021/bi9022126

  日期：2010.5.11

  BtrN catalyzes the two-electron oxidation of the C3 secondary alcohol of 2-deoxy-scyllo-inosamine to the corresponding ketone and is a member of a subclass of radical S-adenosylmethionine (SAM) enzymes called radical SAM (RS) dehydrogenases. Like all RS enzymes, BtrN contains a [4Fe-4S] cluster that delivers an electron to SAM, inducing its cleavage to the common intermediate in RS reactions, the 5'-deoxyadenosyl 5'-radical. In this work, we show that BtrN contains an additional [4Fe-4S] cluster, thought to bind in contact with the substrate to facilitate loss of the second electron in the two-electron oxidation.
• Characterization and Mechanistic Study of a Radical SAM Dehydrogenase in the Biosynthesis of Butirosin
  作者：Kenichi Yokoyama、Mario Numakura、Fumitaka Kudo、Daijiro Ohmori、Tadashi Eguchi

  DOI：10.1021/ja072481t

  日期：2007.12.1

  and dideuterated 5'-deoxyadenosines proved the reversibility of the hydrogen abstraction step. The present study suggests that BtrN is an unusual radical SAM dehydrogenase catalyzing the oxidation of the hydroxyl group by a radical mechanism. This is the first report of the mechanistic study on the oxidation of a hydroxyl group by a radical SAM enzyme.

  在butirosin 生物合成基因簇中编码的BtrN 具有在自由基S-腺苷甲硫氨酸(SAM) 超家族中保守的CXXXCXXC 基序。其在butirosin 生产者环状芽孢杆菌中的基因破坏导致2-脱氧青蟹肌胺(DOIA) 和2-脱氧链霉胺(DOS) 之间的生物合成途径中断。此外，过表达酶的体外测定表明，BtrN 在严格厌氧条件下催化 DOIA 的氧化，同时消耗等摩尔量的 SAM 以产生 5'-脱氧腺苷、甲硫氨酸和 3-氨基-2,3-双脱氧-青蟹肌糖（氨基-DOI）。动力学分析显示底物被 DOIA 抑制，但不被 SAM 抑制，这表明反应是有序 Bi Ter 机制，SAM 是第一个底物，DOIA 是第二个底物。BtrN 与 [3-2 H] DOIA 反应生成非标记、单氘和双氘 5'-脱氧腺苷，而未通过在氧化氘缓冲液中孵育非标记 DOIA 而掺入氘。这些结果表明，DOIA 的 C-3 处的氢原子直接转移到