1,2-Dihydroxy-5-(methylthio)pent-1-en-3-one | 746507-19-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 1,2-Dihydroxy-5-(methylthio)pent-1-en-3-one
• 英文别名: (Z)-1,2-dihydroxy-5-methylsulfanylpent-1-en-3-one
• CAS: 746507-19-7
• 化学式: C₆H₁₀O₃S
• 分子量: 162.21
• InChiKey: CILXJJLQPTUUSS-XQRVVYSFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  10
• 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：
  82.8
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  1,2-Dihydroxy-5-(methylthio)pent-1-en-3-one 、 氧气 生成 α-keto-γ-methylthio-butyrate 、 草氨酸 、 氢(+1)阳离子
  参考文献：
  名称：

  肺炎克雷伯氏菌蛋氨酸抢救途径中两种双加氧酶的机理研究。

  摘要：

  从肺炎克雷伯菌中克隆了两个双加氧酶（ARD和ARD'），它们催化高级aci还原酮中间体CH（3）SCH（2）CH（2）COCH（OH）= CH（OH）的不同氧化分解反应（I ），在蛋氨酸抢救途径中。这两种酶的显着之处在于它们具有相同的多肽序列，但结合不同的金属离子（分别为Ni（2+）和Fe（2+））。ARD将I转换为CH（3）SCH（2）CH（2）COOH，CO和HCOOH。ARD'将I转换为CH（3）SCH（2）CH（2）COCOOH和HCOOH。动力学分析表明ARD和ARD'都具有顺序机制。模型底物（II）（I的脱硫类似物）首先与酶结合，这通过结合时其λ（最大）红移来证明。II形成的二价阴离子引起相同的λ（max）红移，表明II形成二价阴离子与酶结合。富电子的二价阴离子可能与O（2）反应形成过氧化物阴离子中间体。以前的（18）O（2）和（14）C示踪剂实验确定ARD将（18）O（2）合

  DOI：

  10.1021/bi010110y
• 作为产物：
  描述：

  5-(Methylthio)-2,3-dioxopentyl phosphate 、 水 生成 1,2-Dihydroxy-5-(methylthio)pent-1-en-3-one 、 H3PO4
  参考文献：
  名称：

  Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase Activity

  摘要：

  Enolase-phosphatase E1 (MASA) is a bifunctional enzyme in the ubiquitous methionine salvage pathway that catalyzes the continuous reactions of 2,3-diketo-5-methylthio-1-phosphopentane to yield the aci-reductone metabolite using Mg2+ as cofactor. In this study, we have determined the crystal structure of MASA and its complex with a substrate analog to 1.7A resolution by multi-wavelength anomalous diffraction and molecular replacement techniques, respectively. The structures support the proposed mechanism of phosphatase activity and further suggest the probable mechanism of enolization. We establish a model for substrate binding to describe in detail the enzymatic reaction and the formation of the transition state, which will provide insight into the reaction mechanisms of other enzymes in the same family.

  DOI：

  10.1016/j.jmb.2005.01.072

文献信息

• XAS Investigation of the Structure and Function of Ni in Acireductone Dioxygenase
  作者：Faizah Al-Mjeni、Tingting Ju、Thomas C. Pochapsky、Michael J. Maroney

  DOI：10.1021/bi012209a

  日期：2002.5.1

  including 3-4 histidine residues, demonstrates that the substrate binds to the Ni center in a bidentate fashion by displacing two ligands, at least one of which is a histidine ligand, and provides insight into the mechanism of catalysis employed by a Ni-containing dioxygenase. Efficiently relaxed and hyperfine-shifted resonances are observed in the (1)H nuclear magnetic resonance spectrum of Ni-ARD that

  乙酰丙二酮双加氧酶（ARDs）是参与蛋氨酸循环途径的酶，可调节细胞周期的各个方面。肺炎克雷伯菌产生两种酶，它们具有共同的多肽序列，但仅存在的金属离子不同。ci啶酮（1,2-二羟基-3-酮-5-甲基硫代戊烯）与Fe-ARD和二氧反应生成甲酸和2-酮-4-甲基硫代丁酸（甲硫氨酸的α-酮酸前体）。Ni-ARD与阿替考酮和双氧反应生成甲硫代丙酸甲酯，CO和甲酸酯，并且不位于蛋氨酸再循环途径上。X射线吸收光谱（XAS）研究了静止的Ni-ARD酶和酶-底物复合物中催化Ni中心的结构。这项研究建立了静止的Ni-ARD中Ni位的结构，其中包含六个配位的Ni位，这些位点由O / N供体配体组成，其中包括3-4个组氨酸残基，表明底物以二齿方式结合Ni中心取代两个配体，其中至少一个是组氨酸配体，并提供了对含镍双加氧酶所采用的催化机理的见解。在Ni-ARD的（1）H核磁共振波谱中观察到有效的弛豫和超精细位移共振，
• Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae
  作者：Thomas C. Pochapsky、Susan Sondej Pochapsky、Tingting Ju、Huaping Mo、Faizah Al-Mjeni、Michael J. Maroney

  DOI：10.1038/nsb863

  日期：2002.12

  Here we report the structure of acireductone dioxygenase (ARD), the first determined for a new family of metalloenzymes. ARD represents a branch point in the methionine salvage pathway leading from methylthioadenosine to methionine and has been shown to catalyze different reactions depending on the type of metal ion bound in the active site. The solution structure of nickel-containing ARD (Ni-ARD) was determined using NMR methods. X-ray absorption spectroscopy, assignment of hyperfine shifted NMR resonances and conserved domain homology were used to model the metal-binding site because of the paramagnetism of the bound Ni2+. Although there is no structure in the Protein Data Bank within 3 Å r.m.s deviation of that of Ni-ARD, the enzyme active site is located in a conserved double-stranded b-helix domain. Furthermore, the proposed Ni-ARD active site shows significant post-facto structural homology to the active sites of several metalloenzymes in the cupin superfamily.

  在此，我们报告了乙酰还原二氧酶（ARD）的结构，这是第一个被确定的新金属酶家族。ARD是甲硫腺苷向甲硫氨酸的蛋氨酸修复途径中的一个分支点，已被证明能够根据活性位点中结合的金属离子的类型催化不同的反应。含镍ARD（Ni-ARD）的溶液结构是通过核磁共振（NMR）方法确定的。由于结合的Ni2+具有顺磁性，因此X射线吸收光谱、超精细核磁共振共振谱的分配和保守域同源性被用于模拟金属结合位点。尽管蛋白质数据库中没有与Ni-ARD结构偏差小于3 Å的，但酶活性位点位于保守的双链β-螺旋结构域中。此外，拟议的Ni-ARD
• A Functional Link Between RuBisCO-like Protein of <i>Bacillus</i> and Photosynthetic RuBisCO
  作者：Hiroki Ashida、Yohtaro Saito、Chojiro Kojima、Kazuo Kobayashi、Naotake Ogasawara、Akiho Yokota

  DOI：10.1126/science.1086997

  日期：2003.10.10

  The genomes of several nonphotosynthetic bacteria, such as Bacillus subtilis , and some Archaea include genes for proteins with sequence homology to the large subunit of ribulose bisphosphate carboxylase/oxygenase (RuBisCO). We found that such a RuBisCO-like protein (RLP) from B. subtilis catalyzed the 2,3-diketo-5-methylthiopentyl-1-phosphate enolase reaction in the methionine salvage pathway. A growth-defective mutant, in which the gene for this RLP had been disrupted, was rescued by the gene for RuBisCOfrom the photosynthetic bacterium Rhodospirillum rubrum . Thus, the photosynthetic RuBisCO from R. rubrum retains the ability to function in the methionine salvage pathway in B. subtilis .

  几种非光合细菌的基因组（如枯草杆菌等）和一些古菌包括具有与核酮糖双磷酸羧化/氧化酶（RuBisCO）大亚基序列同源性的蛋白质基因。我们发现，来自枯草杆菌的这种类RuBisCO蛋白质（RLP）在蛋氨酸拯救途径中催化2,3-二酮-5-甲基硫代戊糖-1-磷酸烯醇酶反应。一个生长缺陷突变体，其中这个RLP基因已被破坏，被光合细菌红螺菌的RuBisCO基因所拯救。因此，来自红螺菌的光合RuBisCO在枯草杆菌中保留了在蛋氨酸拯救途径中发挥作用的能力。
• Genes and uses thereof to modulate secondary metabolite biosynthesis
  申请人：Inze G. Dirk

  公开号：US20060041962A1

  公开（公告）日：2006-02-23

  The present invention relates to the use of a genome wide expression profiling technology in combination with the detection of the presence of secondary metabolites of interest to isolate genes that can be used to modulate the production of secondary metabolites in organisms and cell lines derived therefrom.

  本发明涉及将基因组全表达谱分析技术与检测相关次生代谢物的存在相结合，分离出可用于调节生物体及其衍生细胞系次生代谢物生产的基因。
• Furfine E.S.; Abeles R.H., J Biol Chem, 1988, 0021-9258, 9598-606
  作者：Furfine E.S.、Abeles R.H.

  DOI：——

  日期：——