4-methyl-2-oxopentanoate | 10250-86-9

• 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: 4-methyl-2-oxopentanoate
• CAS: 10250-86-9
• 化学式: C₆H₉O₃
• 分子量: 129.136
• InChiKey: BKAJNAXTPSGJCU-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  1.6
• 重原子数：
  9
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  57.2
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  4-methyl-2-oxopentanoate 在 formate dehydrogenase 、 phenylalanine dehydrogenase ammonium formate 、 三羟甲基氨基甲烷盐酸盐 、 nicotinamide adenine dinucleotide 作用下， 以 水 为溶剂， 反应 24.0h， 以83%的产率得到L-亮氨酸
  参考文献：
  名称：

  Asano, Yasuhisa; Nakazawa, Akiko, Agricultural and Biological Chemistry, 1987, vol. 51, # 7, p. 2035 - 2036

  摘要：

  DOI：
• 作为产物：
  描述：

  α-hydroxyisohexanoate 以1.57 mmol的产率得到(S)-2-Hydroxy-4-methyl-pentanoic acid anion
  参考文献：
  名称：

  Skopan, Haike; Guenther, Helmut; Simon, Helmut, Angewandte Chemie, 1987, vol. 99, # 2, p. 139 - 141

  摘要：

  DOI：

文献信息

• Effects of Gln102Arg and Cys97Gly mutations on the structural specificity and stereospecificity of the L-lactate dehydrogenase from Bacillus stearothermophilus
  作者：Helmut K. W. Kallwass、Marcel A. Luyten、Wendy Parris、Marvin Gold、Cyril M. Kay、J. Bryan Jones

  DOI：10.1021/ja00038a016

  日期：1992.6

  The L-lactate dehydrogenase of Bacillus stearothermophilus (BSLDH) is a thermostable enzyme with considerable potential for applications in asymmetric synthesis. An understanding of the factors controlling its structural specificity and stereospecificity is therefore of interest. In this paper the effects of GIn 102→Arg and Cys97→Gly mutations have been evaluated. In a survey of thirteen 2-keto acids

  嗜热脂肪芽孢杆菌 (BSLDH) 的 L-乳酸脱氢酶是一种热稳定酶，在不对称合成中具有相当大的应用潜力。因此，了解控制其结构特异性和立体特异性的因素是很有意义的。本文评估了 GIn 102→Arg 和 Cys97→Gly 突变的影响。在对 13 种 2-酮酸的调查中，发现 Q102R 突变降低了 BSLDH 还原具有小或亲水 R 基团的 RCOCOOH 底物的活性，而不影响其对具有较大疏水性 R 取代基的那些的活性
• Thermodynamics of reactions catalysed by branched-chain-amino-acid transaminase
  作者：Yadu B. Tewari、Robert N. Goldberg、J.David Rozzell

  DOI：10.1006/jcht.2000.0686

  日期：2000.10

  Abstract Apparent equilibrium constants and calorimetric enthalpies of reaction have been measured for reactions catalysed by branched-chain-amino-acid transaminase. The following biochemical reactions have been studied at the temperature 298.15 K and in the pH range (7.15 to 7.24):l-valine(aq) + 2-oxoglutarate(aq) = 2-oxoisovalerate(aq) + l-glutamate(aq);l-leucine(aq) + 2-oxoglutarate(aq) = 2-oxoisocaproate(aq)

  摘要 测量了支链氨基酸转氨酶催化反应的表观平衡常数和反应热焓。在温度 298.15 K 和 pH 范围（7.15 至 7.24）下研究了以下生化反应：l-缬氨酸（aq）+ 2-氧代戊二酸（aq）= 2-氧代异戊酸（aq）+ l-谷氨酸（aq） ;l-亮氨酸(aq) + 2-氧代戊二酸(aq) = 2-氧代异己酸(aq) + l-谷氨酸(aq); 和叔-亮氨酸(aq) + 2-氧代戊二酸(aq) = 3,3-二甲基-2-氧代丁酸(aq) + l-谷氨酸(aq)。结果已用于计算涉及特定物种的参考反应的平衡常数和标准摩尔焓 ΔrHmo、熵 ΔrSmo 和吉布斯自由能 ΔrGmochanges。还计算了这些反应在生理条件下的表观平衡常数和标准转换吉布斯自由能变化。讨论了使用这些结果优化支链氨基酸的产品产量。
• 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family
  作者：María-José Bonete、Juan Ferrer、Carmen Pire、Magdalena Penades、José Luiz Ruiz

  DOI：10.1016/s0300-9084(00)01193-7

  日期：2000.12

  An NAD-dependent D-2-hydroxyacid dehydrogenase (EC 1.1.1.) was isolated and characterized from the halophilic Archaeon Haloferax mediterranei. The enzyme is a dimer with a molecular mass of 101.4 +/- 3.3 kDa. It is strictly NAD-dependent and exhibits its highest activity in 4 M NaCl. The enzyme is characterized by a broad substrate specificity 2-ketoisocaproate and 2-ketobutyrate being the substrates

  从嗜盐古细菌Haloferax mediterranei中分离并鉴定了NAD依赖性D-2-羟酸脱氢酶（EC 1.1.1）。该酶是分子量为101.4 +/- 3.3 kDa的二聚体。它严格依赖NAD，并且在4 M NaCl中表现出最高的活性。该酶的特征在于具有广泛的底物特异性，2-酮异己酸和2-酮丁酸是具有更高的Vmax / Km的底物。当丙酮酸和2-酮丁酸为底物时，最佳pH为酸性（pH 5），而对于2-酮异己酸根，在7.5至8.5的碱性pH值下可获得最大活性。最佳温度为52摄氏度，在65摄氏度时活性明显降低。这种新酶可用于生产D-2-羟基羧酸。
• Snake Venom L-Amino Acid Oxidases: Trends in Pharmacology and Biochemistry
  作者：Luiz Fernando M. Izidoro、Juliana C. Sobrinho、Mirian M. Mendes、Tássia R. Costa、Amy N. Grabner、Veridiana M. Rodrigues、Saulo L. da Silva、Fernando B. Zanchi、Juliana P. Zuliani、Carla F. C. Fernandes、Leonardo A. Calderon、Rodrigo G. Stábeli、Andreimar M. Soares

  DOI：10.1155/2014/196754

  日期：——

  L-amino acid oxidases are enzymes found in several organisms, including venoms of snakes, where they contribute to the toxicity of ophidian envenomation. Their toxicity is primarily due to enzymatic activity, but other mechanisms have been proposed recently which require further investigation. L-amino acid oxidases exert biological and pharmacological effects, including actions on platelet aggregation and the induction of apoptosis, hemorrhage, and cytotoxicity. These proteins present a high biotechnological potential for the development of antimicrobial, antitumor, and antiprotozoan agents. This review provides an overview of the biochemical properties and pharmacological effects of snake venom L-amino acid oxidases, their structure/activity relationship, and supposed mechanisms of action described so far.

  L-氨基酸氧化酶是一种酶，存在于多种生物体中，包括蛇毒中，其中它们对蛇毒的毒性起着贡献。它们的毒性主要是由于酶活性，但最近提出了其他机制，需要进一步研究。L-氨基酸氧化酶对血小板聚集和诱导凋亡、出血和细胞毒性等具有生物学和药理学作用。这些蛋白质具有高度的生物技术潜力，可用于开发抗微生物、抗肿瘤和抗原虫药物。本综述概述了蛇毒L-氨基酸氧化酶的生化特性和药理学效应，它们的结构/活性关系以及迄今为止所描述的假定作用机制。
• Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II
  作者：Qian Han、Tao Cai、Danilo A. Tagle、Howard Robinson、Jianyong Li

  DOI：10.1042/bsr20080085

  日期：2008.8.1

  KAT (kynurenine aminotransferase) II is a primary enzyme in the brain for catalysing the transamination of kynurenine to KYNA (kynurenic acid). KYNA is the only known endogenous antagonist of the N-methyl-D-aspartate receptor. The enzyme also catalyses the transamination of aminoadipate to α-oxoadipate; therefore it was initially named AADAT (aminoadipate aminotransferase). As an endotoxin, aminoadipate influences various elements of glutamatergic neurotransmission and kills primary astrocytes in the brain. A number of studies dealing with the biochemical and functional characteristics of this enzyme exist in the literature, but a systematic assessment of KAT II addressing its substrate profile and kinetic properties has not been performed. The present study examines the biochemical and structural characterization of a human KAT II/AADAT. Substrate screening of human KAT II revealed that the enzyme has a very broad substrate specificity, is capable of catalysing the transamination of 16 out of 24 tested amino acids and could utilize all 16 tested α-oxo acids as amino-group acceptors. Kinetic analysis of human KAT II demonstrated its catalytic efficiency for individual amino-group donors and acceptors, providing information as to its preferred substrate affinity. Structural analysis of the human KAT II complex with α-oxoglutaric acid revealed a conformational change of an N-terminal fraction, residues 15–33, that is able to adapt to different substrate sizes, which provides a structural basis for its broad substrate specificity.

  KAT（犬尿氨酸氨基转移酶）Ⅱ是大脑中催化犬尿氨酸转化为 KYNA（犬尿酸）的主要酶。KYNA 是唯一已知的 N-甲基-D-天冬氨酸受体内源性拮抗剂。这种酶还能催化氨基己二酸向α-氧代己二酸的转化，因此最初被命名为 AADAT（氨基己二酸氨基转移酶）。作为一种内毒素，氨基己二酸盐会影响谷氨酸能神经传递的各种因素，并杀死大脑中的原发性星形胶质细胞。文献中有许多关于这种酶的生物化学和功能特性的研究，但尚未对 KAT II 的底物概况和动力学特性进行系统评估。本研究探讨了人 KAT II/AADAT 的生化和结构特征。人 KAT II 的底物筛选显示，该酶具有非常广泛的底物特异性，能够催化 24 种测试氨基酸中 16 种氨基酸的转氨基反应，并能利用所有 16 种测试的 α-氧代酸作为氨基基团接受体。对人类 KAT II 的动力学分析表明了它对单个氨基基团供体和受体的催化效率，从而提供了有关其首选底物亲和性的信息。对人 KAT II 与 α-oxoglutaric acid 复合物的结构分析表明，其 N 端部分残基 15-33 发生了构象变化，能够适应不同大小的底物，这为其广泛的底物特异性提供了结构基础。