2-hydroxy-4-oxobutane-1,2,4-tricarboxylate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate
• 英文别名: 4-carboxy-4-hydroxy-2-oxoadipate
• 化学式: C₇H₅O₈
• 分子量: 217.112
• InChiKey: RQMCNDRMPZBEOD-UHFFFAOYSA-K

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  15
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  158
• 氢给体数：
  1
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  2-hydroxy-4-oxobutane-1,2,4-tricarboxylate 生成 piruvate 、 2-氧代丁二酸
  参考文献：
  名称：

  邻苯二甲酸酯生长的och假单胞菌4-羟基-4-甲基-2-氧代戊二酸醛缩酶的纯化和性质。

  摘要：

  4-羟基-4-甲基-2-氧代戊二酸醛缩酶[4-羟基-4-甲基-2-氧代戊二酸丙酮酸裂合酶：EC 4.1.3.17]已纯化至均一（纯化约770倍，收率11.4％）在邻苯二甲酸盐上生长的och假单胞菌。该酶的分子量为160,000（在Bio-Gel A-1.5m上进行凝胶过滤），亚单位分子量为26,000（SDS-PAGE），等电点为5.0（等电聚焦）。该酶需要二价金属离子（例如Mg2 +，Mn2 +，Co2 +，Zn2 +和Cd2 +）才能发挥活性。该酶主动裂解酶的生理底物4-羧基-4-羟基-2-氧代己二酸酯，得到丙酮酸和草酰乙酸，但对4-羟基-4-甲基-2-氧代戊二酸酯显示出低得多的亲和力。低速切割4-羟基-2-氧代戊二酸酯以丙酮酸和乙醛酸酯化。优先切割底物的l-异构体，而不是极化测定的d-异构体。酶反应是可逆的：HMG和HG裂解反应的平衡常数（pH 8.0、25 C）分别约为0.07和0

  DOI：

  10.1093/oxfordjournals.jbchem.a123201

文献信息

• Purification and Properties of 2-Pyrone-4,6-Dicarboxylate Hydrolase
  作者：Kiyofumi MARUYAMA

  DOI：10.1093/oxfordjournals.jbchem.a134210

  日期：1983.2

  A hydrolase which catalyzes specifically the interconversion between 2-pyrone-4,6-dicarboxylate and 4-oxalmesaconate was purified about 410-fold with a 16% yield from cell-free extracts of Pseudomonas ochraceae grown with phthalate. Upon disc gel electrophoresis, the enzyme preparation gave a single band which was coincident with the enzyme activity. The molecular weight of the enzyme was estimated

  从邻苯二甲酸酯生长的无假单胞菌提取物中，水解催化特定水解2-吡喃酮4,6-二羧酸酯和4-草酸酯的水解酶约410倍，收率16％。经圆盘凝胶电泳后，酶制剂产生一条与酶活性一致的条带。通过在Sephadex G-75上进行凝胶过滤，估计该酶的分子量为31,000，通过十二烷基硫酸钠凝胶电泳估计该酶的分子量为33,000。通过等电聚焦测定该酶的等电点为pH 5.49。该酶对2-pyrone-4,6-dicarboxylate具有特异性，而其他各种内酯均不能用作底物。2-吡喃酮4-，6-二羧酸酯水解，4-草酸酯的形成和质子产生的化学计量约为1：1：1。水解和合成2-pyrone-4,6-dicarboxylate的最佳pH分别为8.5和6.0。2-pyrone-4,6-dicarboxylate和4-oxalmesaconate的Km值分别为87和26 microM。在pH 8.5下，处于平衡状态的
• Purification and Properties of 4-Hydroxy-4-Methyl-2-Oxoglutarate Aldolase from Pseudomonas ochraceae Grown on Phthalate
  作者：Kiyofumi Maruyama

  DOI：10.1093/oxfordjournals.jbchem.a123201

  日期：1990.8

  4-Hydroxy-4-methyl-2-oxoglutarate aldolase [4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase: EC 4.1.3.17] has been purified to homogeneity (about 770-fold purification, yield 11.4%) from Pseudomonas ochraceae grown on phthalate. The enzyme has a molecular weight of 160,000 (gel filtration on Bio-Gel A-1.5m), a subunit molecular weight of 26,000 (SDS-PAGE) and an isoelectric point of 5.0 (isoelectric

  4-羟基-4-甲基-2-氧代戊二酸醛缩酶[4-羟基-4-甲基-2-氧代戊二酸丙酮酸裂合酶：EC 4.1.3.17]已纯化至均一（纯化约770倍，收率11.4％）在邻苯二甲酸盐上生长的och假单胞菌。该酶的分子量为160,000（在Bio-Gel A-1.5m上进行凝胶过滤），亚单位分子量为26,000（SDS-PAGE），等电点为5.0（等电聚焦）。该酶需要二价金属离子（例如Mg2 +，Mn2 +，Co2 +，Zn2 +和Cd2 +）才能发挥活性。该酶主动裂解酶的生理底物4-羧基-4-羟基-2-氧代己二酸酯，得到丙酮酸和草酰乙酸，但对4-羟基-4-甲基-2-氧代戊二酸酯显示出低得多的亲和力。低速切割4-羟基-2-氧代戊二酸酯以丙酮酸和乙醛酸酯化。优先切割底物的l-异构体，而不是极化测定的d-异构体。酶反应是可逆的：HMG和HG裂解反应的平衡常数（pH 8.0、25 C）分别约为0.07和0
• The 4-Oxalomesaconate Hydratase Gene, Involved in the Protocatechuate 4,5-Cleavage Pathway, Is Essential to Vanillate and Syringate Degradation in <i>Sphingomonas paucimobilis</i> SYK-6
  作者：Hirofumi Hara、Eiji Masai、Yoshihiro Katayama、Masao Fukuda

  DOI：10.1128/jb.182.24.6950-6957.2000

  日期：2000.12.15

  Sphingomonas paucimobilis SYK-6 is able to grow on various dimeric lignin compounds, which are converted to vanillate and syringate by the actions of unique lignin degradation enzymes in this strain. Vanillate and syringate are degraded by the O -demethylase and converted into protocatechuate (PCA) and 3- O -methylgallate (3MGA), respectively. PCA is further degraded via the PCA 4,5-cleavage pathway, while the results suggested that 3MGA is degraded through another pathway in which PCA 4,5-dioxygenase is not involved. In a 10.5-kb Eco RI fragment carrying the genes for PCA 4,5-dioxygenase ( ligAB ), 2-pyrone-4,6-dicarboxylate hydrolase ( ligI ), and a portion of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase ( ligC ), we found the ligJ gene encoding 4-oxalomesaconate (OMA) hydratase, which catalyzes the conversion of OMA into 4-carboxy-4-hydroxy-2-oxoadipate. The ligJ gene is transcribed in the same direction as ligABC genes and consists of an 1,023-bp open reading frame encoding a polypeptide with a molecular mass of 38,008 Da, which is located 73-bp upstream from ligA . The ligJ gene product (LigJ), expressed in Escherichia coli , was purified to near homogeneity and was estimated to be a homodimer (69.5 kDa) by gel filtration chromatography. The isoelectric point was determined to be 4.9, and the optimal temperature is 30°C. The K _m for OMA and the V _max were determined to be 138 μM and 440 U/mg, respectively. LigJ activity was inhibited by the addition of thiol reagents, suggesting that some cysteine residue is part of the catalytic site. The ligJ gene disruption in SYK-6 caused the growth defect on and the accumulation of common metabolites from both vanillate and syringate, indicating that the ligJ gene is essential to the degradation of these two compounds. These results indicated that syringate is converted into OMA via 3MGA, and it enters the PCA 4,5-cleavage pathway.

  摘要 Sphingomonas paucimobilis SYK-6 能够在各种二聚木质素化合物上生长，并在该菌株独特的木质素降解酶的作用下转化为香草酸和丁香酸。香草酸酯和丁香酸酯通过 O -脱甲基酶降解，转化成原儿茶酸盐（PCA）和 3- O -甲基棓酸盐（3MGA）。PCA 通过 PCA 4,5-裂解途径进一步降解，而结果表明 3MGA 是通过另一种途径降解的，PCA 4,5-二氧酶并不参与其中。在一个 10.5-kb Eco RI 片段中，携带有 PCA 4,5-二氧合酶基因（ligAB ligAB )、2-吡喃酮-4,6-二羧酸水解酶( ligI )、2-吡喃酮-4,6-二羧酸水解酶(ligI)、4-羧基-2-羟基琥珀酸-6-半醛脱氢酶(ligC)的部分基因。 ligC )，我们发现 基因 基因，该基因可催化 OMA 转化为 4-羧基-4-羟基-2-氧代己二酸。该基因 ligJ 基因的转录方向与 基因的转录方向相同。 基因的转录方向相同，由一个 1,023 bp 的开放阅读框组成，编码一个分子质量为 38,008 Da 的多肽。 ligA .其 基因产物 基因产物（LigJ）在 大肠杆菌中表达 经凝胶过滤色谱法纯化后接近均一，估计为同源二聚体（69.5 kDa）。等电点为 4.9，最佳温度为 30°C。其 K m 和 V 最大值 分别为 138 μM 和 440 U/mg 。加入硫醇试剂后，LigJ 的活性受到抑制，这表明某些半胱氨酸残基是催化位点的一部分。在 ligJ 基因干扰导致了 SYK-6 在香草酸和丁香酸盐上的生长缺陷和常见代谢产物的积累，表明 ligJ 基因对这两种化合物的降解至关重要。这些结果表明，丁香酸盐通过 3MGA 转化为 OMA，并进入 PCA 4,5 裂解途径。
• Purification and properties of γ-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate
  作者：Kiyofumi Maruyama

  DOI：10.1016/0006-291x(85)91674-2

  日期：1985.4

  Pseudomonas ochraceae produced inducibly a hydro-lyase which catalyzes the reversible conversion of gamma-oxalomesaconate into (-)-gamma-oxalocitramalate. The enzyme has been purified to homogeneity from the bacteria grown with phthalate. The enzyme was a dimeric protein (pI=4.9) with a Mr of 68,000 and showed a high specificity for gamma-oxalomesaconate (Km=14 microM) and (-)-gamma-oxalocitramalate

  草假单胞菌可诱导地产生一种水解酶，该酶催化γ-草酰胺酸可逆转化为（-）-γ-草酸过苹果酸酯。该酶已从与邻苯二甲酸酯一起生长的细菌中纯化至同质。该酶是二聚体蛋白（pI = 4.9），Mr为68,000，并且对γ-草酰氨基乙酸（Km = 14 microM）和（-）-γ-草酸金属苹果酸酯（Km = 6.4 microM）表现出高特异性。在pH值为8.0和24摄氏度下，γ-草酰氨基磺酸水合的平衡常数为2.5。各种硫醇激活了酶。
• Enzymes Responsible for Degradation of 4-Oxalmesaconic Acid in Pseudomonas ochraceae
  作者：Kiyofumi MARUYAMA

  DOI：10.1093/oxfordjournals.jbchem.a134211

  日期：1983.2

  The enzyme responsible for the degradation of 4-oxalmesaconate was partially purified from Pseudomonas ochraceae grown with phthalate. Column chromatography on DEAE-cellulose caused separation into two distinct enzymes, I and II. 4-Oxalmesaconate was converted into pyruvate and oxalacetate in the presence of MgCl2 and enzymes I and II. Optimum pH of the reaction was observed at pH 8.2 in Tris-HCl buffer

  从与邻苯二甲酸酯一起生长的草假单胞菌中部分纯化了负责降解4-草酰胺酸的酶。在DEAE-纤维素上进行柱色谱分离可分为两种不同的酶I和II。在存在MgCl2以及酶I和II的情况下，将4-草酸二十烷酸酯转化为丙酮酸和草酰乙酸。在Tris-HCl缓冲液中，在pH 8.2处观察到反应的最佳pH。MgCl2可以用MnCl2或CoCl2代替。两种酶在65℃下对10分钟的热处理均稳定。酶反应的时间过程，产物和底物特异性的分析解释了两种酶的功能。酶I（分子量为55,000，等电点为5.1）将4-草酸马考酸盐水合，得到4-草酰草酸盐，可以分类为水解酶。酵素II（160,000，5。0）在存在MgCl 2的条件下，催化4-草酰草酸酯的醛糖裂解为丙酮酸和草酰乙酸。酶II还将4-羟基-4-甲基-2-氧代戊二酸酯裂解为丙酮酸。酶反应的化学计量表明，酶II催化的裂解仅在底物的一种对映异构体上发生。此外，与其他工作人员先