3-methylthioptopropionate | 168650-25-7

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 3-methylthioptopropionate
• 英文别名: 3-(methylthio)propanoate；3-(Methylthio)propionate；3-methylsulfanylpropanoate
• CAS: 168650-25-7
• 化学式: C₄H₇O₂S
• 分子量: 119.164
• InChiKey: CAOMCZAIALVUPA-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  7
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  65.4
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  3-methylthioptopropionate 、 氯 反应 0.67h， 以to obtain a Cl2 -MMPA molar ratio的产率得到Cl2 MMPA
  参考文献：
  名称：

  Process for the preparation of isothiazolone

  摘要：

  2-甲基异噻唑啉-3-酮（5H-MIT）和5-氯-2-甲基异噻唑啉-3-酮（5Cl-MIT）的混合物是通过在卤代溶剂中连续操作中使用氯气对N-甲基-3-巯基丙酰胺（MMPA）进行氯化制备的。

  公开号：

  US05315008A1
• 作为产物：
  描述：

  3-甲硫基丙酸甲酯 生成 3-methylthioptopropionate
  参考文献：
  名称：

  Visser, Pieter T.; Kiene, Ronald P.; Taylor, Barrie F., FEMS Microbiology Ecology, 1994, vol. 14, # 2, p. 179 - 190

  摘要：

  DOI：

文献信息

• 2 + 1 Chelating Systems for Binding Organometallic Fragment Tc(CO) 3 +
  作者：N. I. Gorshkov、A. A. Lumpov、A. E. Miroslavov、D. N. Suglobov

  DOI：10.1007/s11137-005-0045-2

  日期：2005.1

  Complexation of 99, 99m Tc(CO) 3 + organometallic fragment with 2 + 1 chelating systems was studied. HPLC analysis showed that the dithiocarbamate complexes of 99m Tc are stronger than their xanthate, acetylacetonate, and γ-methoxycarbonylmethylacetylacetonate analogs. To block the third vacancy in the technetium coordination sphere, we studied thiols, thioethers, primary and secondary amines, hydroxyl ion, imidazole, phosphines, and isocyanides. As determined by 99m Tc NMR spectroscopy, the mixed-ligand complexes Tc(CO)3(DTC)L (DTC is dithiocarbamate and L is isocyanide, imidazole, and phosphine) are the most stable to the histidine challenge reaction. HPLC analysis showed that, among these 2 + 1 systems, only the DTC-isonitrile system forms a single complex with 99m Tc(CO) 3 + . The minimal dithiocarbamate-isocyanide concentration providing complete binding of 99m Tc(CO) 3 + is 10−4 M.

  研究了 99、99m Tc(CO) 3 + 有机金属片段与 2 + 1 螯合体系的络合。高效液相色谱分析显示，99m Tc 的二硫代氨基甲酸盐络合物比黄原酸盐、乙酰丙酮酸盐和γ-甲氧羰基甲基乙酰丙酮酸盐类似物更强。为了阻止锝配位球中的第三个空位，我们研究了硫醇、硫醚、伯胺和仲胺、羟基离子、咪唑、膦和异氰酸酯。根据 99m Tc NMR 光谱测定，混合配体配合物 Tc(CO)3(DTC)L（DTC 为二硫代氨基甲酸酯，L 为异氰酸酯、咪唑和膦类）对组氨酸挑战反应最稳定。高效液相色谱分析显示，在这些 2 + 1 系统中，只有 DTC- 异腈系统与 99m Tc(CO) 3 + 形成单一复合物。能与 99m Tc(CO) 3 + 完全结合的最小二硫代氨基甲酸-异氰酸酯浓度为 10-4 M。
• Mechanistic Studies of Two Dioxygenases in the Methionine Salvage Pathway of <i>Klebsiella pneumoniae</i>^,
  作者：Yong Dai、Thomas C. Pochapsky、Robert H. Abeles

  DOI：10.1021/bi010110y

  日期：2001.5.1

  five-membered cyclic peroxide intermediate for ARD and a four-membered cyclic peroxide intermediate for ARD'. A model chemical reaction demonstrates the chemical and kinetic competency of the proposed five-membered cyclic peroxide intermediate. The breakdown of the four-membered and five-membered cyclic peroxide intermediates gives the ARD' and ARD products, respectively. The nature of the metal ion appears to

  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
• 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
• Dimethylsulfoniopropionate-Dependent Demethylase (DmdA) from <i>Pelagibacter ubique</i> and <i>Silicibacter pomeroyi</i>
  作者：Chris R. Reisch、Mary Ann Moran、William B. Whitman

  DOI：10.1128/jb.00770-08

  日期：2008.12.15

  The ubiquitous algal metabolite dimethylsulfoniopropionate (DMSP) is a major source of carbon and reduced sulfur for marine bacteria. Recently, the enzyme responsible for the demethylation of DMSP, designated DmdA, was identified, and homologs were found to be common in marine bacterioplankton cells. The recombinant DmdA proteins from the cultured marine bacteria Pelagibacter ubique HTCC1062 and Silicibacter pomeroyi DSS-3 were purified with a three-step procedure using anion-exchange, hydrophobic interaction, and hydroxyapatite chromatographies. The P. ubique enzyme possessed an M _r on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of 38,500. Under nondenaturing conditions, the M _r was 68,000, suggesting that the enzyme was likely to be a dimer. The purified enzyme exhibited strict substrate specificity for DMSP, as DmdA from both S. pomeroyi and P. ubique possessed no detectable demethylase activity with glycine betaine, dimethyl glycine, methylmercaptopropionate, methionine, or dimethylsulfonioacetate. Less than 1% activity was found with dimethylsulfoniobutanoate and dimethylsulfoniopentanoate. The apparent K _m s for DMSP were 13.2 ± 2.0 and 5.4 ± 2.3 mM for the P. ubique and S. pomeroyi enzymes, respectively. In cell extracts of S. pomeroyi DSS-3, the apparent K _m for DMSP was 8.6 ± 1.2 mM, similar to that of purified recombinant DmdA. The intracellular concentration of DMSP in chemostat-grown S. pomeroyi DSS-3 was 70 mM. These results suggest that marine bacterioplankton may actively accumulate DMSP to osmotically significant concentrations that favor near-maximal rates of DMSP demethylation activity.

  摘要 无处不在的藻类代谢物二甲基硫代丙酸酯（DMSP）是海洋细菌的主要碳源和还原硫。最近，一种被命名为 DmdA 的负责 DMSP 去甲基化的酶被鉴定出来，并且发现同源物在海洋浮游细菌细胞中很常见。从培养的海洋细菌中获得的重组 DmdA 蛋白 Pelagibacter ubique HTCC1062 和 Silicibacter pomeroyi DSS-3 的重组 DmdA 蛋白采用阴离子交换、疏水相互作用和羟基磷灰石色谱三步法进行纯化。结果表明 P. ubique 酶具有 M r 为 38 500。在非变性条件下 M r 为 68,000，表明该酶可能是二聚体。纯化的酶对 DMSP 表现出严格的底物特异性，因为 DmdA 既来自 S. pomeroyi，也来自 S. pomeroyi。 和 和 P. ubique 在甘氨酸甜菜碱、二甲基甘氨酸、巯基丙酸甲酯、蛋氨酸或二甲基磺酰乙酸中均未检测到去甲基化酶活性。二甲基砜基丁酸酯和二甲基砜基戊酸酯的活性不到 1%。表观活性 K m 分别为 13.2 ± 2.0 毫摩尔和 5.4 ± 2.3 毫摩尔。 P. ubique 和 pomeroyi 分别为 13.2 ± 2.0 mM 和 5.4 ± 2.3 mM。在 S. pomeroyi DSS-3 中，表观 K m 为 8.6 ± 1.2 mM，与纯化的重组 DmdA 相似。在恒温培养箱中生长的 DSS-3 的细胞内浓度为 70 mM。 DSS-3 细胞内的 DMSP 浓度为 70 mM。这些结果表明，海洋浮游细菌可能会积极积累 DMSP，使其达到显著的渗透压浓度，从而有利于接近最大速率的 DMSP 去甲基化活动。