2-pyrazinecarboxylate anion | 61288-78-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 2-pyrazinecarboxylate anion
• 英文别名: 2-pyrazinoic acid anion；2-pyrazinecarboxylate；Pyrazine-2-carboxylate
• CAS: 61288-78-6
• 化学式: C₅H₃N₂O₂
• 分子量: 123.091
• InChiKey: NIPZZXUFJPQHNH-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  9
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  65.9
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  、 2-pyrazinecarboxylate anion 在 2,6-二甲基吡啶 作用下， 以 乙二醇甲醚 、 水 为溶剂， 以72%的产率得到Ru⁽²⁺⁾*2(C₆H₅(CH)2C₅H₃N)2*C₄H₃N₂(COO)^(1-)*PF₆^(1-)=[Ru((C₆H₅(CH)2C₅H₃N)2)2(C₄H₃N₂(COO))]PF₆
  参考文献：
  名称：

  Leidner; Sullivan, B. Patrick; Reed, Inorganic Chemistry, 1987, vol. 26, # 6, p. 882 - 891

  摘要：

  DOI：
• 作为产物：
  描述：

  2,3-吡嗪二羧酸 在 水 作用下， 反应 24.0h， 生成 草酸酯 、 2-pyrazinecarboxylate anion
  参考文献：
  名称：

  Photoluminescent Lanthanide-Organic Bilayer Networks with 2,3-Pyrazinedicarboxylate and Oxalate

  摘要：

  The hydrothermal reaction between lanthanide nitrates and 2,3-pyrazinedicarboxylic acid led to a new series of two-dimensional (2D) lanthanide-organic frameworks: [Ln(2)(2,3-pzdc)(2)(ox)(H2O2](n)[where 2,3-pzdc2 = 2,3-pyrazinedicarboxylate, ox(2-) = oxalate, and Ln(III) = Ce, Nd, Sm, Eu, Gd, Tb, or Er]. The structural details of these materials were determined by single-crystal X-ray diffraction (for Ce3+ and Nd3+) that revealed the formation of a layered structure. Cationic monolayers of if {(2)(infinity)n(2,3-pzdc)(H2O](+)} are interconnected via the ox 2 ligand leading to the formation of neutral Ln2(2,3-pzdc)(2)(ox)(H2O2] bilayer networks; structural cohesion of the crystalline packing is reinforced by the presence of highly directional 0 H " " 0 hydrogen bonds between adjacent bilayers. Under the employed hydrothermal conditions 2,3-pyrazinedicarboxylic acid can be decomposed into ox(2) and 2-pyrazinecarboxylate (2-pzc), as unequivocally proved by the isolation of the discrete complex ITb2(2pzO(4)(ox)(H2O)(6) ]" (H2O)-H-10 Single-crystal X-ray diffraction of this latter complex revealed its co-crystallization with an unprecedented (H2O)(16) water cluster. Photoluminescence measurements were performed for the Nd3(+), Sm3+, Eu3+, and Tb3+ compounds which show, under UV excitation at room temperature, the Ln(3+) characteristic intra-4f(N) emission peaks. The energy level of the triplet states of 2,3-pyrazinedicarboxylic acid (18939 cm(-1)) and oxalic acid (24570 cm(-1)) was determined from the 12K emission spectrum of the Gd3+ compound. The D-5(0) and D-3(4) lifetime values (0.333 +/- 0.006 and 0.577 +/- 0.017 ms) and the absolute emission guantum yields (0.13 +/- 0.01 and 0.05 +/- 0.01) were determined for the Eu3+ and Tb3+ compounds, respectively. For the Eu3+ compound the energy transfer efficiency arising from the ligands' excited states was estimated (0.93 +/- 0.01).

  DOI：

  10.1021/ic902522j

文献信息

• Identification, cloning, and expression of the Escherichia coli pyrazinamidase and nicotinamidase gene, pncA
  作者：R Frothingham、W A Meeker-O'Connell、E A Talbot、J W George、K N Kreuzer

  DOI：10.1128/aac.40.6.1426

  日期：1996.6

  Pyrazinamide (PZA) is one of the three most important drugs for treatment of Mycobacterium tuberculosis infections. The antibacterial activity of PZA requires a bacterial enzyme, pyrazinamidase (PZAase), which hydrolyzes PZA to form pyrazinoic acid and ammonia. Most PZA-resistant clinical M. tuberculosis isolates lack PZAase activity. With the goal of eventually identifying and characterizing the M.tuberculosis PZAase gene, we began with the more tractable organism, Escherichia coli, which also has PZAase activity. We screened a transposon-generated E. coli insertion mutant library, using a qualitative PZAase assay. Two PZAase-negative mutants out of 4,000 colonies screened were identified. In each mutant, the transposon interrupted the same 639-bp open reading frame (ORF), ORF1. The expression of ORF1 on a multicopy plasmid complemented a PZAase-negative mutant, leading to PZAase activity levels approximately 10-fold greater than those of the wild type. PZA has a structure similar to that of nicotinamide, a pyridine nucleotide cycle intermediate, so we tested our strains for nicotinamidase activity (EC 3.5.1.19) (genetic locus pncA). The construct with multiple plasmid copies of ORF1 had an approximately 10-fold increase in levels of nicotinamidase activity. This overexpressing strain could utilize nicotinamide as a sole nitrogen source, through wild-type E. coli cannot. We conclude that a single E. coli enzyme accounts for both PZAase and nicotinamidase activities and that ORF1 is the E.coli PZAase and nicotinamidase gene, pncA.

  吡嗪酰胺（PZA）是治疗结核分枝杆菌感染的三种最重要药物之一。PZA 的抗菌活性需要一种细菌酶，即吡嗪酰胺酶（PZAase），它能水解 PZA 生成吡嗪酸和氨。大多数耐 PZA 的临床结核杆菌分离株缺乏 PZA 酶活性。为了最终鉴定结核杆菌的 PZAase 基因并确定其特性，我们从更易处理的大肠杆菌入手，因为大肠杆菌也具有 PZAase 活性。我们使用定性 PZAase 检测法筛选了转座子产生的大肠杆菌插入突变体文库。在筛选出的 4000 个菌落中，我们发现了两个 PZAase 阴性突变体。在每个突变体中，转座子都打断了相同的 639-bp 开放阅读框（ORF），即 ORF1。ORF1 在多拷贝质粒上的表达补充了 PZAase 阴性突变体，使 PZAase 活性水平比野生型高出约 10 倍。PZA 的结构与吡啶核苷酸循环中间体烟酰胺相似，因此我们检测了菌株的烟酰胺酶活性（EC 3.5.1.19）（遗传位点 pncA）。含有多个 ORF1 质粒拷贝的构建体的烟酰胺酶活性水平提高了约 10 倍。这种过表达菌株可以利用烟酰胺作为唯一的氮源，而野生型大肠杆菌则不能。我们的结论是，大肠杆菌中只有一种酶同时具有 PZAase 和烟酰胺酶活性，ORF1 就是大肠杆菌的 PZAase 和烟酰胺酶基因 pncA。
• Crystal Structure and Mechanism of Catalysis of a Pyrazinamidase from <i>Pyrococcus horikoshii</i>
  作者：Xinlin Du、Weiru Wang、Rosalind Kim、Hisao Yakota、Huy Nguyen、Sung-Hou Kim

  DOI：10.1021/bi0115479

  日期：2001.11.1

  Loss of PZAase activity is the major mechanism of pyrazinamide-resistance by M. tuberculosis. We have determined the crystal structure of the gene product of Pyrococcus horikoshii 999 (PH999), a PZAase, and its complex with zinc ion by X-ray crystallography. The overall fold of PH999 is similar to that of N-carbamoylsarcosine amidohydrolase (CSHase) of Arthrobacter sp. and YcaC of Escherichia coli, a protein

  细菌吡嗪酰胺酶（PZAase）/烟酰胺酰胺酶将吡嗪酰胺（PZA）转化为氨和吡嗪酸，对结核分枝杆菌有活性。PZAase活性的丧失是结核分枝杆菌抵抗吡嗪酰胺的主要机制。我们已经通过X射线晶体学确定了Pyrococcus horikoshii 999（PH999），PZAase及其与锌离子的复合物的基因产物的晶体结构。PH999的总体折叠与节杆菌属的N-氨基甲酰基肌氨酸酰胺水解酶（CSHase）相似。和大肠杆菌的YcaC，一种生理功能未知的蛋白质。通过在CSHase和YcaC的活性位点中也存在的结构特征来识别PH999的活性位点：三联体（D10，K94和C133）和顺式肽（在V128和A129之间）。出奇，一个金属离子结合位点被发现在活性位点，随后被PH999与Zn（2+）络合的晶体结构所证实。提出了三联体，顺式肽和金属离子在催化中的作用。由于PH999和结核分枝杆菌的PZAase之间具有广泛的
• Expression of <i>Mycobacterium smegmatis</i> Pyrazinamidase in <i>Mycobacterium tuberculosis</i> Confers Hypersensitivity to Pyrazinamide and Related Amides
  作者：Helena I. M. Boshoff、Valerie Mizrahi

  DOI：10.1128/jb.182.19.5479-5485.2000

  日期：2000.10

  A pyrazinamidase (PZase)-deficient pncA mutant of Mycobacterium tuberculosis , constructed by allelic exchange, was used to investigate the effects of heterologous amidase gene expression on the susceptibility of this organism to pyrazinamide (PZA) and related amides. The mutant was highly resistant to PZA (MIC, >2,000 μg/ml), in accordance with the well-established role of pncA in the PZA susceptibility of M. tuberculosis (A. Scorpio and Y. Zhang, Nat. Med. 2:662–667, 1996). Integration of the pzaA gene encoding the major PZase/nicotinamidase from Mycobacterium smegmatis (H. I. M. Boshoff and V. Mizrahi, J. Bacteriol. 180:5809–5814, 1998) or the M. tuberculosis pncA gene into the pncA mutant complemented its PZase/nicotinamidase defect. In both pzaA - and pncA -complemented mutant strains, the PZase activity was detected exclusively in the cytoplasm, suggesting an intracellular localization for PzaA and PncA. The pzaA -complemented strain was hypersensitive to PZA (MIC, ≤10 μg/ml) and nicotinamide (MIC, ≥20 μg/ml) and was also sensitive to benzamide (MIC, 20 μg/ml), unlike the wild-type and pncA -complemented mutant strains, which were highly resistant to this amide (MIC, >500 μg/ml). This finding was consistent with the observation that benzamide is hydrolyzed by PzaA but not by PncA. Overexpression of PzaA also conferred sensitivity to PZA, nicotinamide, and benzamide on M. smegmatis (MIC, 150 μg/ml in all cases) and rendered Escherichia coli hypersensitive for growth at low pH.

  摘要 一种吡嗪酰胺酶（PZase）缺陷的 pncA 突变体 结核分枝杆菌 通过等位基因交换构建的 pncA 缺失突变体，用于研究异源酰胺酶基因表达对该生物体对吡嗪酰胺（PZA）及相关酰胺类药物敏感性的影响。该突变体对 PZA 具有高度抗性（MIC, >2,000μg/ml），这与已证实的 pncA 对 PZA 结核杆菌 (A.Scorpio和Y.Zhang，Nat.Med.2:662-667，1996）。整合 pzaA 基因的整合。 分枝杆菌的 (H. I. M. Boshoff 和 V. Mizrahi，J. Bacteriol. 结核杆菌 pncA 基因转化为 pncA 突变体的 PZase/烟酰胺酶缺陷。在这两种 pzaA - 和 pncA -互补突变株中，PZ酶活性只在细胞质中被检测到，这表明 PzaA 和 PncA 在细胞内定位。在 pzaA -互补的菌株对 PZA（MIC, ≤10 μg/ml）和烟酰胺（MIC, ≥20 μg/ml）不敏感，对苯甲酰胺（MIC, 20 μg/ml）也不敏感，这与野生型和 pncA -互补突变株对这种酰胺具有高度抗性（MIC，500 μg/ml）。这一发现与苯甲酰胺可被 PzaA 而非 PncA 水解的观察结果一致。过表达 PzaA 也会使烟曲霉菌对 PZA、烟酰胺和苯甲酰胺敏感。 M. smegmatis (的敏感性（所有情况下的 MIC 均为 150 μg/ml），并使 大肠杆菌 对在低 pH 值条件下的生长不敏感。
• Zhang, Songsheng; Holl, Lori A.; Shepherd, Rex E., Inorganic Chemistry, 1990, vol. 29, # 5, p. 1012 - 1022
  作者：Zhang, Songsheng、Holl, Lori A.、Shepherd, Rex E.

  DOI：——

  日期：——
• Leidner; Sullivan, B. Patrick; Reed, Inorganic Chemistry, 1987, vol. 26, # 6, p. 882 - 891
  作者：Leidner、Sullivan, B. Patrick、Reed、White、Crimmins、Murray, Royce W.、Meyer, Thomas J.

  DOI：——

  日期：——