(3R)-3r,4t,5c-trihydroxy-cyclohexane-1,2-dione | 949461-91-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (3R)-3r,4t,5c-trihydroxy-cyclohexane-1,2-dione
• 英文别名: (3R)-3r,4t,5c-Trihydroxy-cyclohexan-1,2-dion；(3R)-3r.4t.5c-Trihydroxy-cyclohexandion-(1.2)；(3R,4S,5R)-3,4,5-trihydroxycyclohexane-1,2-dione
• CAS: 949461-91-0
• 化学式: C₆H₈O₅
• 分子量: 160.127
• InChiKey: SHFQRUVRUBHHRE-CJPQEGFPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.6
• 重原子数：
  11
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  94.8
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (3R)-3r,4t,5c-trihydroxy-cyclohexane-1,2-dione 、 苯肼 生成 (3S)-3r,4t,5c-trihydroxy-cyclohexane-1,2-dione-bis-phenylhydrazone
  参考文献：
  名称：

  研究了一系列的环十二醇。荚膜糖醇的配置

  摘要：

  欧莱雅风情的各种反应montrant que le viburnitolreprésentele 2,3,5 / 4,6-6-环已烷-戊醇。

  DOI：

  10.1002/hlca.19500330218
• 作为产物：
  描述：

  原栎醇 在 水 作用下， 生成 (3R)-3r,4t,5c-trihydroxy-cyclohexane-1,2-dione
  参考文献：
  名称：

  研究了一系列的环十二醇。荚膜糖醇的配置

  摘要：

  欧莱雅风情的各种反应montrant que le viburnitolreprésentele 2,3,5 / 4,6-6-环已烷-戊醇。

  DOI：

  10.1002/hlca.19500330218

文献信息

• Identification of two scyllo-inositol dehydrogenases in Bacillus subtilis
  作者：Tetsuro Morinaga、Hitoshi Ashida、Ken-ichi Yoshida

  DOI：10.1099/mic.0.037499-0

  日期：2010.5.1

  scyllo-Inositol (SI) is a stereoisomer of inositol whose catabolism has not been characterized in bacteria. We found thatBacillus subtilis168 was able to grow using SI as its sole carbon source and that this growth was dependent on a functionalioloperon for catabolism ofmyo-inositol (MI; another inositol isomer, which is abundant in nature). Previous studies elucidated the MI catabolic pathway inB. subtilisas comprising multiple stepwise reactions catalysed by a series of Iol enzymes. The first step of the pathway converts MI toscyllo-inosose (SIS) and involves the MI dehydrogenase IolG. Since IolG does not act on SI, we suspected that there could be another enzyme converting SI into SIS, namely an SI dehydrogenase. Within the whole genome, seven genes paralogous toiolGhave been identified and two of these,iolXandiolW(formerly known asyisSandyvaA, respectively), were selected as candidate genes for the putative SI dehydrogenase since they were both prominently expressed whenB. subtiliswas grown on medium containing SI.iolXandiolWwere cloned inEscherichia coliand both were shown to encode a functional enzyme, revealing the two distinct SI dehydrogenases inB. subtilis. Since inactivation ofiolXimpaired growth with SI as the carbon source, IolX was identified as a catabolic enzyme required for SI catabolism and it was shown to be NAD⁺dependent. The physiological role of IolW remains unclear, but it may be capable of producing SI from SIS with NADPH oxidation.

  scyllo-肌醇(SI)是肌醇的立体异构体，其在细菌中的分解代谢尚未被表征。我们发现Bacillus subtilis168能够利用SI作为其唯一的碳源生长，并且该生长依赖于功能性的iol操纵子来代谢myo-肌醇(MI；另一种在自然界中丰富的肌醇异构体)。以前的研究阐明了B. subtilis中MI代谢途径由一系列Iol酶催化的多步反应组成。途径的第一步将MI转化为scyllo-肌醇糖(SIS)，并涉及MI脱氢酶IolG。由于IolG不作用于SI，我们怀疑可能存在另一种酶将SI转化为SIS，即SI脱氢酶。在整个基因组中，已经鉴定出与iolG同源的七个基因，其中两个，iolX和iolW（以前分别称为yisS和yvaA），被选为假定的SI脱氢酶的候选基因，因为它们在含有SI的培养基中生长时都表达明显。iolX和iolW被克隆到Escherichia coli中，并且两者都被证明编码一种功能性酶，揭示了B. subtilis中两种不同的SI脱氢酶。由于iolX失活会影响以SI为碳源的生长，因此确定了IolX作为SI代谢所需的代谢酶，并且它被证明是NAD⁺依赖的。IolW的生理作用尚不清楚，但它可能能够通过NADPH氧化从SIS产生SI。
• The fifth gene of the iol operon of Bacillus subtilis, iolE, encodes 2-keto-myo-inositol dehydratase
  作者：Ken-ichi Yoshida、Masanori Yamaguchi、Hideki Ikeda、Kaoru Omae、Ken-ichi Tsurusaki、Yasutaro Fujita

  DOI：10.1099/mic.0.26768-0

  日期：2004.3.1

  The myo-inositol catabolism pathway of Bacillus subtilis has not been fully characterized but was proposed to involve step-wise multiple reactions that finally yielded acetyl-CoA and dihydroxyacetone phosphate. It is known that the iolABCDEFGHIJ operon is responsible for the catabolism of inositol. IolG catalyses the first step of myo-inositol catabolism, the dehydrogenation of myo-inositol, producing 2-keto-myo-inositol (inosose). The second step was thought to be the dehydration of inosose. Genetic and biochemical analyses of the iol genes led to the identification of iolE, encoding the enzyme for the second step of inositol catabolism, inosose dehydratase. The reaction product of inosose dehydratase was identified as d-2,3-diketo-4-deoxy-epi-inositol.

  枯草芽孢杆菌的肌醇分解代谢途径尚未完全确定，但据推测，该途径涉及多个步骤，最终生成乙酰辅酶A和二羟基丙酮磷酸。已知iolABCDEFGHIJ基因组负责肌醇的分解代谢。IolG催化肌醇分解代谢的第一步，即肌醇脱氢，生成2-酮肌醇（肌苷）。第二步被认为是肌苷脱水。通过对iol基因进行遗传和生化分析，确定了iolE，它编码肌醇分解代谢第二步所需的酶——肌苷脱水酶。肌苷脱水酶的反应产物被确定为d-2,3-二酮-4-脱氧-表肌醇。
• Identification of a Functional 2-keto-<i>myo</i>-Inositol Dehydratase Gene of<i>Sinorhizobium fredii</i>USDA191 Required for<i>myo</i>-Inositol Utilization
  作者：Ken-ichi YOSHIDA、Won-Seok KIM、Masaki KINEHARA、Rie MUKAI、Hitoshi ASHIDA、Hideki IKEDA、Yasutaro FUJITA、Hari B. KRISHNAN

  DOI：10.1271/bbb.60362

  日期：2006.12.23

  Sinorhizobium fredii USDA191 is a Gram-negative bacterium capable of forming nitrogen-fixing nodules on soybean roots. The USDA191 idhA gene encoding myo-inositol dehydrogenase, an enzyme necessary for myo-inositol utilization, is known to be involved in competitive nodulation and nitrogen fixation. In Bacillus subtilis, myo-inositol dehydrogenase catalyzes the first step of the myo-inositol catabolic pathway. Recently iolE was identified as the gene encoding 2-keto-myo-inositol dehydratase, which catalyzes the second step in the pathway. Here we report the presence of 2-keto-myo-inositol dehydratase activity in free-living USDA191 cells cultured in a medium containing myo-inositol. An iolE ortholog was cloned from USDA191. USDA191 iolE was expressed in Escherichia coli as a His6-tag fusion and purified to exhibit 2-keto-myo-inositol dehydratase activity. Inactivation of USDA191 iolE led to defective myo-inositol utilization. USDA191 iolE partially complemented a B. subtilis iolE deficient mutant. These results suggest that S. fredii USDA191 utilizes a myo-inositol catabolic pathway, analogous to that of B. subtilis, involving at least idhA and iolE.

  Sinorhizobium fredii USDA191是一种革兰氏阴性细菌，能够在大豆根部形成固氮根瘤。已知编码肌醇脱氢酶的USDA191 idhA基因参与竞争性根瘤形成和固氮作用，肌醇脱氢酶是肌醇利用所必需的一种酶。在枯草芽孢杆菌中，肌醇脱氢酶催化肌醇分解代谢途径的第一步。最近，iolE被确定为编码2-酮肌醇脱水酶的基因，该酶催化该途径的第二步。在这里，我们报告了在含有肌醇的培养基中培养的游离USDA191细胞中存在2-酮肌醇脱水酶活性。从USDA191中克隆了iolE同源物。USDA191 iolE在大肠杆菌中以His6标签融合物的形式表达，并纯化以显示2-酮肌醇脱水酶活性。USDA191 iolE的失活导致肌醇利用缺陷。USDA191 iolE部分补充了枯草芽孢杆菌iolE缺陷突变体。这些结果表明，S. fredii USDA191利用肌醇分解代谢途径，类似于枯草芽孢杆菌的肌醇分解代谢途径，至少涉及idhA和iolE。
• Magasanik; Chargaff, Journal of Biological Chemistry, 1948, vol. 174, p. 173,176, 179
  作者：Magasanik、Chargaff

  DOI：——

  日期：——
• myo-Inositol Catabolism in Bacillus subtilis
  作者：Ken-ichi Yoshida、Masanori Yamaguchi、Tetsuro Morinaga、Masaki Kinehara、Maya Ikeuchi、Hitoshi Ashida、Yasutaro Fujita

  DOI：10.1074/jbc.m708043200

  日期：2008.4

  The iolABCDEFGHIJ operon of Bacillus subtilis is responsible for myo-inositol catabolism involving multiple and stepwise reactions. Previous studies demonstrated that IolG and IolE are the enzymes for the first and second reactions, namely dehydrogenation of myo-inositol to give 2-keto-myo-inositol and the subsequent dehydration to 3D-(3,5/4)-trihydroxycyclohexane1,2- dione. In the present studies the third reaction was shown to be the hydrolysis of 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione catalyzed by IolD to yield 5-deoxy-D-glucuronic acid. The fourth reaction was the isomerization of 5-deoxy-D-glucuronic acid by IolB to produce 2-deoxy-5-keto-D-gluconic acid. Next, in the fifth reaction 2-deoxy-5-keto-D-gluconic acid was phosphorylated by IolC kinase to yield 2-deoxy-5-keto-D-gluconic acid 6-phosphate. IolR is known as the repressor controlling transcription of the iol operon. In this reaction 2-deoxy-5-keto-D-gluconic acid 6-phosphate appeared to be the intermediate acting as inducer by antagonizing DNA binding of IolR. Finally, IolJ turned out to be the specific aldolase for the sixth reaction, the cleavage of 2-deoxy-5-keto-D-gluconic acid 6-phosphate into dihydroxyacetone phosphate and malonic semialdehyde. The former is a known glycolytic intermediate, and the latter was previously shown to be converted to acetyl-CoA and CO2 by a reaction catalyzed by IolA. The net result of the inositol catabolic pathway in B. subtilis is, thus, the conversion of myo-inositol to an equimolar mixture of dihydroxyacetone phosphate, acetyl-CoA, and CO2.