Ammonioacetone

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: Ammonioacetone
• 英文别名: 2-oxopropylazanium
• 化学式: C3H8NO+
• 分子量: 74.1
• InChiKey: BCDGQXUMWHRQCB-UHFFFAOYSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  5
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  44.7
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  Ammonioacetone 、 水 、 氧气 生成 双氧水 、 丙酮醛 、 铵
  参考文献：
  名称：

  摘要：

  DOI：
• 作为产物：
  描述：

  L-2-amino-3-oxobutanoate 、 氢(+1)阳离子 生成 Ammonioacetone 、 二氧化碳
  参考文献：
  名称：

  Highly Thermostable L-Threonine Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis

  摘要：

  l-苏氨酸脱氢酶是l-苏氨酸代谢的关键酶，催化NAD+依赖性l-苏氨酸向2-氨基-3-酮丁酸的转化，后者非酶性脱羧生成氨基丙酮。对超嗜热古菌Thermococcus kodakaraensis的基因组序列进行搜索后发现，存在与古细菌和细菌l-苏氨酸脱氢酶基因密切相关的同源物（TK0916）。在大肠杆菌中表达TK0916基因产物并进行纯化和表征后发现，该基因实际上编码一种具有高水平的l-苏氨酸脱氢酶活性的蛋白质（7.26 U mg-1）。该酶在pH 12和90°C时表现出最高的活性。在50°C时，l-苏氨酸和NAD+的Km值分别为1.6 mM和0.028 mM。酶的活性取决于二价阳离子。在85°C时，酶的半衰期超过2小时，在沸水中为24分钟。这是迄今为止报道的最热稳定的苏氨酸脱氢酶，在最高pH（12）下表现出最佳活性。这是首次报道对Thermococcus属的TDH进行表征。

  DOI：

  10.1093/jb/mvp051

文献信息

• Microbial metabolism of amino ketones. <scp>l</scp>-1-aminopropan-2-ol dehydrogenase and <scp>l</scp>-threonine dehydrogenase in <i>Escherichia coli</i>
  作者：JM Turner

  DOI：10.1042/bj1040112

  日期：1967.7.1

  intermediary metabolites and substrate analogues have no effect on the oxidation of dl-1-aminopropan-2-ol to aminoacetone by washed-cell suspensions of Escherichia coli. Only dl-2-hydroxy-2-phenylethylamine, dl-1,3-diaminopropan-2-ol, dl-serine and l-1-(3,4-dihydroxyphenyl)-2-aminoethanol act as inhibitors. 2. Dialysed cell-free extracts of E. coli exhibit an NAD(+)-dependent dl-1-aminopropan-2-ol-dehydrogenase

  1.多种中间产物和底物类似物对大肠杆菌洗涤过的细胞悬浮液将dl-1-氨基丙烷-2-醇氧化为氨基丙酮没有影响。仅dl-2-羟基-2-苯基乙胺，dl-1,3-二氨基丙烷-2-醇，dl-丝氨酸和l-1-（3,4-二羟基苯基）-2-氨基乙醇用作抑制剂。透析后的大肠杆菌无细胞提取物显示出约NAD（+）依赖性的dl-1-氨基丙烷-2-醇-脱氢酶活性。形成8摩尔氨基丙酮/毫克。蛋白质/分钟 在最佳pH值下 10.辅酶和dl-氨基醇的K（m）值约为10。分别为0.4和10.0mm。在pH7.0-7.2时出现较小的活性峰，在pH7时NAD（+）的K（m）约为10。0.05毫米 3. dl-2-羟基-2-苯乙胺，dl-1-氨基丙烷-2抑制无细胞提取物中的酶活性，3-二醇和dl-丝氨酸。dl-苯基丝氨酸和dl-1-氨基丁烷-2-醇被氧化为以氨基酮形式反应的化合物。4.在新鲜的无细胞提取物中，l（+）-1-氨基丙
• L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: gene cloning and enzymatic characterization
  作者：Yasuhiro Shimizu、Haruhiko Sakuraba、Ryushi Kawakami、Shuichiro Goda、Yutaka Kawarabayasi、Toshihisa Ohshima

  DOI：10.1007/s00792-005-0447-2

  日期：2005.8

  A gene encoding the L-threonine dehydrogenase homologue has been identified in a hyperthermophlic archaeon Pyrococcus horikoshii OT3 via genome sequencing. The gene was cloned and expressed in Escherichia coli. The purified enzyme from the recombinant E. coli was extremely thermostable; the activity was not lost after incubation at 100 degrees C for 20 min. The enzyme ( molecular mass: 192 kDa) is composed of a tetrameric structure with a type of subunit ( 41 kDa). The enzyme is specific for NAD and utilizes L-threonine, L-serine and DL-threo-3-phenylserine as the substrate. The enzyme required divalent cations such as Zn2+, Mn2+ and Co2+ for the activity, and contained one zinc ion/subunit. The K-m values for L-threonine and NAD at 50 degrees C were 0.20 mM and 0.024 mM, respectively. Kinetic analyses indicated that the L-threonine oxidation reaction proceeds via a random mechanism with regard to the binding of L-threonine and NAD. The enzyme showed pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of NADH. This is the first description of the characteristics of an L-threonine dehydrogenase from the archaea domain.
• Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
  作者：Noriko Higashi、Harumi Fukada、Kazuhiko Ishikawa

  DOI：10.1263/jbb.99.175

  日期：2005.2

  In the genome data base of the hyperthermophilic archaeon Pyrococcus horikoshii, an open reading frame with sequence homology to a gene encoding alcohol dehydrogenase was found. It was demonstrated that the encoded enzyme was a thermostable L-threonine dehydrogenase which can oxidize the hydroxy alkyl residue of L-threonine associated with the reduction of NAD(+) or NADP'. This enzyme is a member of the zinc-containing L-threonine dehydrogenase family. One enzyme molecule contained one zinc atom, and this metal was considered to contribute to the hyperthermostablility of the enzyme. The reaction of the enzyme proceeded via a sequential mechanism. The Michaelis constants (K-m) for L-threonine and NAD(+) were 0.013 and 0.010 mM, respectively, and the maximum reaction rate (V-max) was 1.75 mmol NADH formed/min/mg-protein at 65 degrees C. The Km values for both L-threonine and NADP(+) were larger than those for L-threonine and NAD(+) with a similar V-max. value. These results indicate that the enzyme has lower affinity to NADP(+) than to NAD(+), and the binding affinity for L-threonine depends on the coenzymes.
• Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon<i>Pyrococcus furiosus</i>
  作者：Ronnie Machielsen、John van der Oost

  DOI：10.1111/j.1742-4658.2006.05290.x

  日期：2006.6

  The gene encoding a threonine dehydrogenase (TDH) has been identified in the hyperthermophilic archaeon Pyrococcus furiosus. The Pf‐TDH protein has been functionally produced in Escherichia coli and purified to homogeneity. The enzyme has a tetrameric conformation with a molecular mass of ≈ 155 kDa. The catalytic activity of the enzyme increases up to 100 °C, and a half‐life of 11 min at this temperature indicates its thermostability. The enzyme is specific for NAD(H), and maximal specific activities were detected with l‐threonine (10.3 U·mg−1) and acetoin (3.9 U·mg−1) in the oxidative and reductive reactions, respectively. Pf‐TDH also utilizes l‐serine and d‐threonine as substrate, but could not oxidize other l‐amino acids. The enzyme requires bivalent cations such as Zn2+ and Co2+ for activity and contains at least one zinc atom per subunit. Km values for l‐threonine and NAD+ at 70 °C were 1.5 mm and 0.055 mm, respectively.
• Epperly B.R.; Dekker E.E., J Biol Chem, 1991, 0021-9258, 6086-92
  作者：Epperly B.R.、Dekker E.E.

  DOI：——

  日期：——