2'-aminobiphenyl-2,3-diol | 148519-91-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2'-aminobiphenyl-2,3-diol
• 英文别名: 3-(2-aminophenyl)benzene-1,2-diol
• CAS: 148519-91-9
• 化学式: C₁₂H₁₁NO₂
• 分子量: 201.225
• InChiKey: WPDDFIBFWKUENN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  15
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  66.5
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2'-aminobiphenyl-2,3-diol 在 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase 、 Tris*HCl buffer 作用下， 生成 2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
  参考文献：
  名称：

  Purification and Characterization ofmeta-Cleavage Compound Hydrolase from a Carbazole DegraderPseudomonas resinovoransStrain CA10

  摘要：

  2-羟基-6-氧代-6-(2'-氨基苯基)-六-2,4-二烯酸[6-(2'-氨基苯基)-HODA]水解酶参与食树脂假单胞菌菌株 CA10 的咔唑降解，从过度表达的大肠杆菌菌株中纯化至接近同质。该酶为二聚体，其最适pH为7.0-7.5。系统发育分析表明该酶与参与单环芳香族化合物降解的其他水解酶有密切关系，并且该酶对2-羟基-6-氧代-6-苯基六-2,4-二烯酸（6-苯基- HODA)，对 2-羟基-6-氧七-2,4-二烯酸和 2-羟基粘康半醛几乎没有活性。对于 6-苯基-HODA（50 mM 磷酸钠，pH 7.5，25°C），该酶的 Km 为 2.51 μM，kcat 为 2.14 (s−1)。发现6-苯基-HODA的苯基部分2'位上的氨基或羟基的存在对酶活性的影响很小；活性降低的顺序为：6-(2'-氨基苯基)-HODA (2.44 U/mg)>6-苯基-HODA (1.99 U/mg)>2-羟基-6-氧代-6-(2' -羟基苯基）-六-2,4-二烯酸（1.05 U/mg）。 2'-取代对活性的影响与基于计算的这些底物的最低未占据分子轨道能量所预测的反应性一致。

  DOI：

  10.1271/bbb.67.36
• 作为产物：
  描述：

  咔唑 在 Escherichia coli JM₁₀₉ 作用下， 以 二甲基亚砜 为溶剂， 反应 18.0h， 以99.1%的产率得到2'-aminobiphenyl-2,3-diol
  参考文献：
  名称：

  Alteration of the Substrate Specificity of the Angular Dioxygenase Carbazole 1,9a-Dioxygenase

  摘要：

  Carbazole 1,9a-二氧化酶（CARDO）由末端氧化酶（CARDO-O）和电子传递组件组成。CARDO能够对多种底物催化特定的氧化反应：对喹啉和二苯并-对-二氧的角氧化，对蒽的侧氧化，以及对弗鲁安的亚甲基碳和二苯并噻吩的硫的单氧化。为了阐明决定其独特底物特异性的分子机制，生成并表征了17个CARDO-O的定点突变体，这些突变体位于氨基酸残基I262、F275、Q282和F329，这些残基通过CARDO-O的晶体结构形成围绕铁活性位点的底物相互作用壁。F329的替换显著降低了氧化活性。然而，几个突变体与野生型酶相比，产生了不同的产物：I262V和Q282Y（1-羟基喹啉），F275W（4-羟基弗鲁安），F275A（未鉴定的弗鲁安烯顺式二氢二醇），以及I262A和I262W（单羟基二苯并噻吩）。这些结果表明，不同底物可能以不同于野生型酶的取向结合在CARDO-O突变体的活性位点。

  DOI：

  10.1271/bbb.80512

文献信息

• Expression, Purification, and Characterization of 2′-Aminobiphenyl-2,3-diol 1,2-dioxygenase from Carbazole-degrader<i>Pseudomonas resinovorans</i>Strain CA10
  作者：Kenichi IWATA、Hideaki NOJIRI、Kentaro SHIMIZU、Takako YOSHIDA、Hiroshi HABE、Toshio OMORI

  DOI：10.1271/bbb.67.300

  日期：2003.1

  The two-subunit meta-cleavage enzyme, 2′-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarBaBb), from the carbazole degrader Pseudomonas resinovorans strain CA10 was purified to homogeneity from an Escherichia coli strain carrying the expression vector pUCA503, in which two copies of the carBaBb genes are tandemly linked. SDS-PAGE and gel filtration showed that CarB was a α2β2-heterotetrameric enzyme with subunit molecular masses of approximately 10,000 for CarBa and 29,000 for CarBb. The optimum pH for activity was 8.5 and that of temperature was 35°C. The CarB enzyme had a Km of 14 μM and a kcat/Km of 0.25 μM−1 s−1 for 2′-aminobiphenyl-2,3-diol, and the catalytic activities for biphenyl-type catecholic substrates were higher than those for monoaromatic catechol derivatives. The enzyme was originally isolated as a meta-cleavage enzyme for 2′-aminobiphenyl-2,3-diol involved in carbazole degradation, but the enzyme was highly specific for 2,3-dihydroxybiphenyl.

  从携带表达载体 pUCA503 的大肠杆菌菌株中纯化了来自咔唑降解菌树脂假单胞菌 CA10 株系的双亚基元裂解酶 2′-氨基联苯-2,3-二醇 1,2-二氧 化酶（CarBaBb）。SDS-PAGE 和凝胶过滤显示，CarB 是一种 α2β2-三聚体酶，CarBa 的亚基分子质量约为 10,000 ，CarBb 的亚基分子质量约为 29,000 。活性的最适 pH 值为 8.5，最适温度为 35°C。CarB 酶对 2′-氨基联苯-2,3-二醇的 Km 为 14 μM，kcat/Km 为 0.25 μM-1 s-1，对联苯类儿茶酚底物的催化活性高于对单芳香族儿茶酚衍生物的催化活性。该酶最初被分离为 2′-氨基联苯-2,3-二醇的元裂解酶，参与咔唑降解，但该酶对 2,3-二羟基联苯具有高度特异性。
• SURFACE MODIFIED COLLOIDAL PARTICLES
  申请人：CLEMSON UNIVERSITY

  公开号：US20130236416A1

  公开（公告）日：2013-09-12

  The present invention generally relates to surface modified colloidal particles. The invention further relates to methods of preparing and methods of using the same.

  本发明通常涉及表面改性的胶体颗粒。本发明还涉及制备和使用这些颗粒的方法。
• Purification and Characterization of Carbazole 1,9a-Dioxygenase, a Three-Component Dioxygenase System of <i>Pseudomonas resinovorans</i> Strain CA10
  作者：Jeong-Won Nam、Hideaki Nojiri、Haruko Noguchi、Hiromasa Uchimura、Takako Yoshida、Hiroshi Habe、Hisakazu Yamane、Toshio Omori

  DOI：10.1128/aem.68.12.5882-5890.2002

  日期：2002.12

  The carbazole 1,9a-dioxygenase (CARDO) system of Pseudomonas resinovorans strain CA10 consists of terminal oxygenase (CarAa), ferredoxin (CarAc), and ferredoxin reductase (CarAd). Each component of CARDO was expressed in Escherichia coli strain BL21(DE3) as a native form (CarAa) or a His-tagged form (CarAc and CarAd) and was purified to apparent homogeneity. CarAa was found to be trimeric and to have one Rieske type [2Fe-2S] cluster and one mononuclear iron center in each monomer. Both His-tagged proteins were found to be monomeric and to contain the prosthetic groups predicted from the deduced amino acid sequence (His-tagged CarAd, one FAD and one [2Fe-2S] cluster per monomer protein; His-tagged CarAc, one Rieske type [2Fe-2S] cluster per monomer protein). Both NADH and NADPH were effective as electron donors for His-tagged CarAd. However, since the k _cat / K _m for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay, NADH was supposed to be the physiological electron donor of CarAd. In the presence of NADH, His-tagged CarAc was reduced by His-tagged CarAd. Similarly, CarAa was reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins could reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc seemed to be indispensable for electron transport, while His-tagged CarAd could be replaced by some unrelated reductases.

  摘要 resinovorans 假单胞菌的咔唑 1,9a-二氧合酶（CARDO）系统 树脂假单胞菌 菌株 CA10 的咔唑 1,9a-二氧化酶（CARDO）系统由末端加氧酶（CarAa）、铁氧还原酶（CarAc）和铁氧还原酶（CarAd）组成。CARDO 的每个组分都在 大肠杆菌 菌株 BL21(DE3)中以原生形式（CarAa）或 His 标记形式（CarAc 和 CarAd）表达 CARDO，并纯化至明显均一。发现 CarAa 为三聚体，每个单体中有一个 Rieske 型 [2Fe-2S] 簇和一个单核铁中心。两种 His 标记的蛋白质均为单体，并含有推导出的氨基酸序列所预测的修复基团（His 标记的 CarAd，每个单体蛋白质含有一个 FAD 和一个 [2Fe-2S] 簇；His 标记的 CarAc，每个单体蛋白质含有一个 Rieske 型 [2Fe-2S] 簇）。对于 His 标记的 CarAd，NADH 和 NADPH 都是有效的电子供体。然而，由于 k cat / K m 在 2,6-二氯苯酚靛酚还原酶试验中，NADH 的 K m 是 NADPH 的 22.3 倍，因此 NADH 应该是 CarAd 的生理电子供体。在 NADH 存在的情况下，His 标记的 CarAc 被 His 标记的 CarAd 还原。同样，CarAa 也被 His 标记的 CarAc、His 标记的 CarAd 和 NADH 还原。这三种纯化蛋白可以在体外重组 CARDO 活性。在重组的 CARDO 系统中，His 标记的 CarAc 似乎是电子传递所不可或缺的，而 His 标记的 CarAd 则可以被一些不相关的还原酶所取代。
• The Genes Coding for the Conversion of Carbazole to Catechol Are Flanked by IS6100 Elements in Sphingomonas sp. Strain XLDN2-5
  作者：Zhonghui Gai、Xiaoyu Wang、Xiaorui Liu、Cui Tai、Hongzhi Tang、Xiaofei He、Geng Wu、Zixin Deng、Ping Xu

  DOI：10.1371/journal.pone.0010018

  日期：——

  Background Carbazole is a recalcitrant compound with a dioxin-like structure and possesses mutagenic and toxic activities. Bacteria respond to a xenobiotic by recruiting exogenous genes to establish a pathway to degrade the xenobiotic, which is necessary for their adaptation and survival. Usually, this process is mediated by mobile genetic elements such as plasmids, transposons, and insertion sequences. Findings The genes encoding the enzymes responsible for the degradation of carbazole to catechol via anthranilate were cloned, sequenced, and characterized from a carbazole-degrading Sphingomonas sp. strain XLDN2-5. The car gene cluster (carRAaBaBbCAc) and fdr gene were accompanied on both sides by two copies of IS6100 elements, and organized as IS6100::ISSsp1-ORF1-carRAaBaBbCAc-ORF8-IS6100-fdr-IS6100. Carbazole was converted by carbazole 1,9a-dioxygenase (CARDO, CarAaAcFdr), meta-cleavage enzyme (CarBaBb), and hydrolase (CarC) to anthranilate and 2-hydroxypenta-2,4-dienoate. The fdr gene encoded a novel ferredoxin reductase whose absence resulted in lower transformation activity of carbazole by CarAa and CarAc. The ant gene cluster (antRAcAdAbAa) which was involved in the conversion of anthranilate to catechol was also sandwiched between two IS6100 elements as IS6100-antRAcAdAbAa-IS6100. Anthranilate 1,2-dioxygenase (ANTDO) was composed of a reductase (AntAa), a ferredoxin (AntAb), and a two-subunit terminal oxygenase (AntAcAd). Reverse transcription-PCR results suggested that carAaBaBbCAc gene cluster, fdr, and antRAcAdAbAa gene cluster were induced when strain XLDN2-5 was exposed to carbazole. Expression of both CARDO and ANTDO in Escherichia coli required the presence of the natural reductases for full enzymatic activity. Conclusions/Significance We predict that IS6100 might play an important role in the establishment of carbazole-degrading pathway, which endows the host to adapt to novel compounds in the environment. The organization of the car and ant genes in strain XLDN2-5 was unique, which showed strong evolutionary trail of gene recruitment mediated by IS6100 and presented a remarkable example of rearrangements and pathway establishments.

  背景咔唑是一种具有类似二恶英结构的难降解化合物，具有诱变和毒性活性。细菌对异生物的反应是通过招募外源基因来建立降解异生物的途径，这是细菌适应和生存所必需的。通常，这一过程是由质粒、转座子和插入序列等移动遗传因子介导的。 研究结果 克隆了负责将咔唑通过蒽酸酯降解为邻苯二酚的酶的基因，并对其进行了测序和表征。car基因簇（carRAaBaBbCAc）和 fdr 基因两侧伴有两个 IS6100 元件拷贝，组成 IS6100::ISSsp1-ORF1-carRAaBaBbCAc-ORF8-IS6100-fdr-IS6100。咔唑在咔唑 1,9a-二加氧酶（CARDO，CaRAaAcFdr）、元裂解酶（CarBaBb）和水解酶（CarC）的作用下转化为蒽酸和 2-羟基戊-2,4-二烯酸酯。fdr 基因编码一种新型铁氧还原酶，缺乏这种酶会导致 CaRAa 和 CaRAc 转化咔唑的活性降低。蚂蚁基因簇（aNTRAcAdAbAa）也夹在两个 IS6100 元素之间，即 IS6100-aNTRAcAdAbAa-IS6100，该基因参与将蒽酸转化为邻苯二酚。蒽酸 1,2-二加氧酶（ANTDO）由还原酶（ANTAa）、铁氧还蛋白（ANTAb）和双亚基末端加氧酶（ANTAcAd）组成。反转录-PCR结果表明，当菌株XLDN2-5暴露于咔唑时，caRAaBaBbCAc基因簇、fdr和aNTRAcAdAbAa基因簇被诱导。CARDO 和 ANTDO 在大肠杆菌中的表达需要天然还原酶的存在才能充分发挥酶的活性。 结论/意义 我们预测，IS6100 可能在咔唑降解途径的建立过程中发挥了重要作用，它赋予了宿主适应环境中新型化合物的能力。菌株 XLDN2-5 中车基因和蚁基因的组织结构非常独特，显示出 IS6100 介导的基因招募的强烈进化痕迹，是基因重排和途径建立的一个显著实例。
• Probe compound for detecting and isolating enzymes and means and methods using the same
  申请人：Helmholtz-Zentrum für Infektionsforschung GmbH

  公开号：EP2230312A1

  公开（公告）日：2010-09-22

  The present invention relates to a probe compound that can comprise any substrate or metabolite of an enzymatic reaction in addition to an indicator component, such as, for example, a fluorescence dye, or the like. Moreover, the present invention relates to means for detecting enzymes in form of an array, which comprises any number of probe compounds of the invention which each comprise a different metabolite of interconnected metabolites representing the central pathways in all forms of life. Moreover, the present invention relates to a method for detecting enzymes involving the application of cell extracts or the like to the array of the invention which leads to reproducible enzymatic reactions with the substrates. These specific enzymatic reactions trigger the indicator (e.g. a fluorescence signal) and bind the enzymes to the respective cognate substrates. Moreover, the invention relates to means for isolating enzymes in form of nanoparticles coated with the probe compound of the invention. The immobilisation of the cognate substrates or metabolites on the surface of nanoparticles by means of the probe compounds allows capturing and isolating the respective enzyme, e.g. for subsequent sequencing.

  本发明涉及一种探针化合物，它可以包括酶反应的任何底物或代谢物，此外还包括指示成分，例如荧光染料或类似物。此外，本发明还涉及以阵列形式检测酶的方法，该阵列由任意数量的本发明探针化合物组成，每种探针化合物由代表所有生命形式中中心途径的相互关联的代谢物中的不同代谢物组成。此外，本发明还涉及一种检测酶的方法，该方法涉及将细胞提取物或类似物应用于本发明的阵列，从而导致与底物发生可重复的酶反应。这些特定的酶反应会触发指示剂（如荧光信号），并将酶与各自的同源底物结合。此外，本发明还涉及以涂覆有本发明探针化合物的纳米颗粒形式分离酶的方法。通过探针化合物将同源底物或代谢物固定在纳米颗粒表面，可以捕获和分离相应的酶，例如用于后续测序。