(4S)-4,6-Dihydroxy-2,5-dioxohexanoate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: (4S)-4,6-Dihydroxy-2,5-dioxohexanoate
• 化学式: C6H7O6-
• 分子量: 175.12
• InChiKey: IBGYNIRCYXIAON-VKHMYHEASA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  12
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  115
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  5-Dehydro-4-deoxy-D-glucuronate 生成 (4S)-4,6-Dihydroxy-2,5-dioxohexanoate
  参考文献：
  名称：

  Novel Insights into E. coli’s Hexuronate Metabolism: KduI Facilitates the Conversion of Galacturonate and Glucuronate under Osmotic Stress Conditions

  摘要：

  我们之前使用无菌小鼠模型，观察了食用富含乳糖饮食的小鼠肠道大肠杆菌中2-脱氧-D-葡萄糖酸3-脱氢酶（KduD）的表达上调，以及食用富含酪蛋白饮食的小鼠肠道大肠杆菌中该酶和5-酮-4-脱氧尿嘧啶异构酶（KduI）的表达下调。本研究旨在确定大肠杆菌蛋白KduD和KduI在体外的作用。在有氧条件下，半乳糖醛酸和葡萄糖醛酸分别诱导kduD和kduI基因表达3倍和7至11倍，而在厌氧条件下，分别诱导9至20倍和19至54倍。KduI促进这些半乳糖醛酸的分解。在大肠杆菌中，半乳糖醛酸和葡萄糖醛酸通常由UxaABC和UxuAB降解。然而，渗透压胁迫以依赖OxyR的方式抑制相应基因的表达。当在存在半乳糖醛酸或葡萄糖醛酸的情况下生长时，与野生型大肠杆菌相比，缺乏KduID的大肠杆菌在渗透压胁迫条件下的最大细胞密度低30%至80%，倍增时间延长1.5至2倍。在乳糖上生长促进细胞内半乳糖醛酸的形成，这可能是KduD在富含乳糖饮食中诱导

  DOI：

  10.1371/journal.pone.0056906

文献信息

• Escherichia coli kduD encodes an oxidoreductase that converts both sugar and steroid substrates
  作者：Agne Tubeleviciute、Mark George Teese、Joachim Jose

  DOI：10.1007/s00253-014-5551-8

  日期：2014.6

  by kduD gene enabled the whole-cell biotransformation of 11-DOC. A 6xHis-tagged version of KduD was purified to homogeneity and found to reduce several eukaryotic steroid hormones and catalyze the conversion of novel sugar substrates. KduD from E. coli is therefore a promiscuous enzyme that has a predicted role in sugar conversion in vivo but can be used for the production of valuable bioactive 20-hydroxysteroids

  以前未鉴定的大肠杆菌氧化还原酶催化将真核甾体激素11-脱氧皮质酮（11-DOC）选择性还原为有价值的生物活性产物4-pregnen-20,21-diol-3-one。实际上，各种NAD（P）H依赖性氧化还原酶可催化C21类固醇的C-20羰基还原。但是，在大肠杆菌中从未描述过具有20-酮类固醇还原酶活性的酶。我们目前的研究旨在鉴定和表征对真核生物类固醇激素11-DOC具有20-酮类固醇还原酶活性的大肠杆菌酶。我们使用蛋白质色谱技术从大肠杆菌DH5α中部分纯化了该酶。质谱显示样品中存在三种NADH特异性氧化还原酶。克隆了编码这些氧化还原酶的基因，并在大肠杆菌UT5600（DE3）中过表达。仅由kduD基因编码的2-dehydro-3-deoxy-D-葡萄糖酸5-dehydrogenase（KduD）的过表达使11-DOC的全细胞生物转化成为可能。纯化的6xHis标记版本的KduD被纯化至均质，
• The crystal structure of 5-keto-4-deoxyuronate isomerase from Escherichia coli
  作者：Robert L. Crowther、Millie M. Georgiadis

  DOI：10.1002/prot.20598

  日期：——
• Analysis of an<i>Erwinia chrysanthemi</i>gene cluster involved in pectin degradation
  作者：G. Condemine、J. Robert-Baudouy

  DOI：10.1111/j.1365-2958.1991.tb02149.x

  日期：1991.9

  SummaryA group of four genes of Erwinia chrysanthemi involved in pectin degradation has been characterized. These four genes form independent transcription units and are regulated by the negative regulatory gene, kdgR. The functions of two of these genes are known: kduD codes for the 2‐keto‐3‐deoxygluconate oxydoreductase and kdul for the 5‐keto‐4‐deoxyuronate isomerase, two enzymes of the pectin degradation pathway. kdgC has 36% homology with pectate lyase genes of the periplasmic family but its product does not seem to have pectinolytic activity. The fourth gene, kdgF, could have a role in the pathogenicity of E. chrysanthemi. A comparison of the regulatory regions of all the genes controlled by kdgR allowed better definition of the KdgR‐binding‐site consensus.
• PREISS J.; ASHWELL G., J Biol Chem, 1963, 0021-9258, 1577-83
  作者：PREISS J.、ASHWELL G.

  DOI：——

  日期：——
• Novel Insights into E. coli’s Hexuronate Metabolism: KduI Facilitates the Conversion of Galacturonate and Glucuronate under Osmotic Stress Conditions
  作者：Monique Rothe、Carl Alpert、Gunnar Loh、Michael Blaut

  DOI：10.1371/journal.pone.0056906

  日期：——

  Using a gnotobiotic mouse model, we previously observed the upregulation of 2-deoxy-D-gluconate 3-dehydrogenase (KduD) in intestinal E. coli of mice fed a lactose-rich diet and the downregulation of this enzyme and of 5-keto 4-deoxyuronate isomerase (KduI) on a casein-rich diet. The present study aimed to define the role of the so far poorly characterized E. coli proteins KduD and KduI in vitro. Galacturonate and glucuronate induced kduD and kduI gene expression 3-fold and 7 to 11-fold, respectively, under aerobic conditions as well as 9 to 20-fold and 19 to 54-fold, respectively, under anaerobic conditions. KduI facilitated the breakdown of these hexuronates. In E. coli, galacturonate and glucuronate are normally degraded by UxaABC and UxuAB. However, osmotic stress represses the expression of the corresponding genes in an OxyR-dependent manner. When grown in the presence of galacturonate or glucuronate, kduID-deficient E. coli had a 30% to 80% lower maximal cell density and 1.5 to 2-fold longer doubling times under osmotic stress conditions than wild type E. coli. Growth on lactose promoted the intracellular formation of hexuronates, which possibly explain the induction of KduD on a lactose-rich diet. These results indicate a novel function of KduI and KduD in E. coli and demonstrate the crucial influence of osmotic stress on the gene expression of hexuronate degrading enzymes.

  我们之前使用无菌小鼠模型，观察了食用富含乳糖饮食的小鼠肠道大肠杆菌中2-脱氧-D-葡萄糖酸3-脱氢酶（KduD）的表达上调，以及食用富含酪蛋白饮食的小鼠肠道大肠杆菌中该酶和5-酮-4-脱氧尿嘧啶异构酶（KduI）的表达下调。本研究旨在确定大肠杆菌蛋白KduD和KduI在体外的作用。在有氧条件下，半乳糖醛酸和葡萄糖醛酸分别诱导kduD和kduI基因表达3倍和7至11倍，而在厌氧条件下，分别诱导9至20倍和19至54倍。KduI促进这些半乳糖醛酸的分解。在大肠杆菌中，半乳糖醛酸和葡萄糖醛酸通常由UxaABC和UxuAB降解。然而，渗透压胁迫以依赖OxyR的方式抑制相应基因的表达。当在存在半乳糖醛酸或葡萄糖醛酸的情况下生长时，与野生型大肠杆菌相比，缺乏KduID的大肠杆菌在渗透压胁迫条件下的最大细胞密度低30%至80%，倍增时间延长1.5至2倍。在乳糖上生长促进细胞内半乳糖醛酸的形成，这可能是KduD在富含乳糖饮食中诱导