H(iminodiacetate)(1-) | 64434-71-5

• 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: H(iminodiacetate)(1-)
• 英文别名: azanediyl-bis-acetic acid; deprotonated form；2-(carboxylatomethylazaniumyl)acetate
• CAS: 64434-71-5
• 化学式: C₄H₆NO₄
• 分子量: 132.096
• InChiKey: NBZBKCUXIYYUSX-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.6
• 重原子数：
  9
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  89.5
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  {Ho(ethylenediaminetetraacetate)}(1-) 、 H(iminodiacetate)(1-) 在 氢氧化钾 作用下， 生成 氢气 、 {Ho(III)-(ethylenediaminetetraacetate)(iminodiacetate)}(3-)
  参考文献：
  名称：

  Kiraly, Robert; Toth, Imre; Zekany, Laszlo, Acta Chimica Hungarica, 1988, vol. 125, # 3, p. 519 - 526

  摘要：

  DOI：
• 作为产物：
  描述：

  1-Deoxy-1-(7,8-dimethyl-2,4-dioxidobenzo[g]pteridin-10(5H)-yl)-5-O-phosphonopentitol 、 nitrilotriacetate 、 氧气 生成 H(iminodiacetate)(1-) 、 FMN 、 glyoxylate 、 水
  参考文献：
  名称：

  Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600

  摘要：

  基于对硝基三乙酸（NTA）消耗的测定，开发了一种测量“Chelatobacter”菌株ATCC 29600细胞提取物中NTA单加氧酶（NTA-Mo）活性并纯化功能性NTA羟化酶复合物的方法。该复合物由两个组分组成，在纯化和稀释过程中容易解离。两个组分均被纯化至95％以上的同质性，并且可以从纯组分A（cA）和组分B（cB）重新构建功能性NTA羟化酶复合物。cB表现出NTA刺激的NADH氧化作用，但无法羟化NTA。它具有88 kDa的原生分子量，并含有单核苷酸黄素（FMN）。cA的原生分子量为99 kDa。尚未证明cA单独具有催化活性。在不利条件下，NADH氧化部分或完全解偶，导致H2O2的形成。最佳羟化活性取决于两个组分的摩尔比，酶复合物的绝对浓度以及FMN的存在。在高盐浓度和黄素腺嘌呤二核苷酸存在下，反应的解偶是有利的。NTA-Mo复合物对巯基试剂敏感，但通过添加过量的二硫苏糖醇可逆抑制。 Mg（2+）-NTA，FMN和NADH的Km值分别确定为0.5 mM，1.3微米和0.35 mM。在26种测试化合物中，NTA是NTA-Mo的唯一底物。

  DOI：

  10.1128/jb.174.4.1179-1188.1992

文献信息

• Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600
  作者：T Uetz、R Schneider、M Snozzi、T Egli

  DOI：10.1128/jb.174.4.1179-1188.1992

  日期：1992.2

  An assay based on the consumption of nitrilotriacetate (NTA) was developed to measure the activity of NTA monooxygenase (NTA-Mo) in cell extracts of "Chelatobacter" strain ATCC 29600 and to purify a functional, NTA-hydroxylating enzyme complex. The complex consisted of two components that easily dissociated during purification and upon dilution. Both components were purified to more than 95% homogeneity, and it was possible to reconstitute the functional, NTA-hydroxylating enzyme complex from pure component A (cA) and component B (cB). cB exhibited NTA-stimulated NADH oxidation but was unable to hydroxylate NTA. It had a native molecular mass of 88 kDa and contained flavin mononucleotide (FMN). cA had a native molecular mass of 99 kDa. No catalytic activity has yet been shown for cA alone. Under unfavorable conditions, NADH oxidation was partly or completely uncoupled from hydroxylation, resulting in the formation of H2O2. Optimum hydroxylating activity was found to be dependent on the molar ratio of the two components, the absolute concentration of the enzyme complex, and the presence of FMN. Uncoupling of the reaction was favored in the presence of high salt concentrations and in the presence of flavin adenine dinucleotide. The NTA-Mo complex was sensitive to sulfhydryl reagents, but inhibition was reversible by addition of excess dithiothreitol. The Km values for Mg(2+)-NTA, FMN, and NADH were determined as 0.5 mM, 1.3 microM, and 0.35 mM, respectively. Of 26 tested compounds, NTA was the only substrate for NTA-Mo.

  基于对硝基三乙酸（NTA）消耗的测定，开发了一种测量“Chelatobacter”菌株ATCC 29600细胞提取物中NTA单加氧酶（NTA-Mo）活性并纯化功能性NTA羟化酶复合物的方法。该复合物由两个组分组成，在纯化和稀释过程中容易解离。两个组分均被纯化至95％以上的同质性，并且可以从纯组分A（cA）和组分B（cB）重新构建功能性NTA羟化酶复合物。cB表现出NTA刺激的NADH氧化作用，但无法羟化NTA。它具有88 kDa的原生分子量，并含有单核苷酸黄素（FMN）。cA的原生分子量为99 kDa。尚未证明cA单独具有催化活性。在不利条件下，NADH氧化部分或完全解偶，导致H2O2的形成。最佳羟化活性取决于两个组分的摩尔比，酶复合物的绝对浓度以及FMN的存在。在高盐浓度和黄素腺嘌呤二核苷酸存在下，反应的解偶是有利的。NTA-Mo复合物对巯基试剂敏感，但通过添加过量的二硫苏糖醇可逆抑制。 Mg（2+）-NTA，FMN和NADH的Km值分别确定为0.5 mM，1.3微米和0.35 mM。在26种测试化合物中，NTA是NTA-Mo的唯一底物。
• Cloning and characterization of the genes encoding nitrilotriacetate monooxygenase of Chelatobacter heintzii ATCC 29600
  作者：H R Knobel、T Egli、J R van der Meer

  DOI：10.1128/jb.178.21.6123-6132.1996

  日期：1996.11

  A 6.2-kb DNA fragment containing the genes for the nitrilotriacetate (NTA) monooxygenase of Chelatobacter heintzii ATCC 29600 was cloned and characterized by DNA sequencing and expression studies. The nucleotide sequence contained three major open reading frames (ORFs). Two of the ORFs, which were oriented divergently with an intergenic region of 307 bp, could be assigned to the NTA monooxygenase components A and B. The predicted N-terminal amino acid sequences of these ORFs were identical with those determined for the purified components. We therefore named these genes ntaA (for component A of NTA monooxygenase) and ntaB (for component B). The ntaA and ntaB genes could be expressed in Escherichia coli DH5alpha, and the gene products were visualized after Western blotting (immunoblotting) and incubation with polyclonal antibodies against component A or B. By mixing overproduced NtaB from E. coli and purified component A from C. heintzii ATCC 29600, reconstitution of a functional NTA monooxygenase complex was possible. The deduced gene product of ntaA showed only significant homology to SoxA (involved in dibenzothiophene degradation) and to SnaA (involved in pristamycin synthesis); that of ntaB shared weak homologies in one domain with other NADH:flavine mononucleotide oxidoreductases. These homologies provide no conclusive answer as to the possible evolutionary origin of the NTA monooxygenase. The deduced gene product of the third ORF (ORF1) had homology in the N-terminal region with the GntR class of bacterial regulator proteins and therefore may encode a regulator protein, possibly involved in regulation of ntaA and ntaB expression.

  一段6.2kb的DNA片段，其中包含Chelatobacter heintzii ATCC 29600的nitrilotriacetate（NTA）单加氧酶基因，经过DNA测序和表达研究进行了克隆和表征。核苷酸序列包含三个主要的开放阅读框架（ORFs）。其中两个ORFs，其定向相反，间隔区为307 bp，可分配给NTA单加氧酶组分A和B。这些ORFs的预测N末端氨基酸序列与纯化组分测定的序列相同。因此，我们将这些基因命名为ntaA（NTA单加氧酶组分A）和ntaB（NTA单加氧酶组分B）。ntaA和ntaB基因可以在大肠杆菌DH5alpha中表达，并且在Western blotting（免疫印迹）和与组分A或B的多克隆抗体孵育后可视化基因产物。通过混合来自大肠杆菌的过量NtaB和来自C. heintzii ATCC 29600的纯化组分A，可以重新组装功能性NTA单加氧酶复合物。ntaA的推导基因产物仅显示与SoxA（参与二苯并噻吩降解）和SnaA（参与普利斯他霉素合成）具有显着同源性；ntaB的推导基因产物在一个领域中与其他NADH：黄素单核苷酸氧化还原酶共享弱同源性。这些同源性并不能提供有关NTA单加氧酶可能的进化起源的确切答案。第三个ORF（ORF1）的推导基因产物在N末端区域具有与细菌调节蛋白GntR类似的同源性，因此可能编码一个调节蛋白，可能参与ntaA和ntaB的表达调节。
• Kiraly, Robert; Toth, Imre; Zekany, Laszlo, Acta Chimica Hungarica, 1988, vol. 125, # 3, p. 519 - 526
  作者：Kiraly, Robert、Toth, Imre、Zekany, Laszlo、Bruecher, Ernoe

  DOI：——

  日期：——
• Cloning, sequencing, and analysis of a gene cluster from Chelatobacter heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase
  作者：Y Xu、M W Mortimer、T S Fisher、M L Kahn、F J Brockman、L Xun

  DOI：10.1128/jb.179.4.1112-1116.1997

  日期：1997.2

  mononucleotide (FMNH2) as reductant; NmoB was similar to an NADH:flavin mononucleotide (FMN) oxidoreductase. On the basis of this information, we tested the function of each component. Purified component B was shown to be an NADH:FMN oxidoreductase, and its activity could be separated from that of component A. When the Photobacterium fischeri NADH:FMN oxidoreductase was substituted for component B in the complete

  三乙酸亚硝酸钠（NTA）是清洁剂中的重要螯合剂，也已广泛用于处理放射性核素。在Hela zii杆菌属ATCC 29600中，NTA的生物降解是由NTA单加氧酶引发的，该酶将NTA氧化为亚氨基二乙酸和乙醛酸。NTA单加氧酶活性需要两个组分蛋白，组分A和组分B，但是每个组分的功能尚不清楚。我们已克隆并测序了编码组件A和B（nmoA和nmoB）以及nmoA下游的两个其他开放阅读框nmoR和nmoT的基因簇。基于序列相似性，nmoR和nmoT可能分别编码调节蛋白和转座酶。NmoA序列类似于单加氧酶，后者使用还原的黄素单核苷酸（FMNH2）作为还原剂；NmoB类似于NADH：黄素单核苷酸（FMN）氧化还原酶。根据这些信息，我们测试了每个组件的功能。纯化的组分B被证明是NADH：FMN氧化还原酶，其活性可以与组分A分开。当费氏杆菌NADH：FMN氧化还原酶在完全反应中代替组分B时，NTA被氧化，表明该