pyrrole-2-carboxylate

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯
• 英文名称: pyrrole-2-carboxylate
• 英文别名: 2-pyrrolecarboxylate；2-PC；1H-Pyrrole-2-carboxylate
• 化学式: C₅H₄NO₂
• 分子量: 110.092
• InChiKey: WRHZVMBBRYBTKZ-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  8
• 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：
  55.9
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  氢(+1)阳离子 、 pyrrole-2-carboxylate 生成 吡咯 、 二氧化碳
  参考文献：
  名称：

  Pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910, an organic-acid-requiring enzyme

  摘要：

  Inducible pyrrole‐2‐carboxylate decarboxylase, which catalyzes the decarboxylation of pyrrole‐2‐carboxylate to pyrrole and CO2 in stoichiometric amounts, was purified from Bacillus megaterium PYR2910. The purity of the enzyme was shown by SDS/PAGE and gel‐permeation HLPC. The enzyme has a molecular mass of approximately 98 kDa and consists of two identical subunits. It is highly specific for pyrrole‐2‐carboxylate, and also catalyzes the reverse reaction, the carboxylation of pyrrole. A unique feature of this enzyme is its requirement of an organic acid, such as acetate, propionate, butyrate or pimelate. A possible catalytic mechanism including a cofactor function of organic acid is discussed.

  DOI：

  10.1046/j.1432-1327.1998.2530480.x
• 作为产物：
  描述：

  吡咯 、 potassium hydrogencarbonate 在 Bacillus megaterium PYR₂₉₁₀ potassium phosphate 、 ammonium acetate 、 sodium ascorbate 作用下， 以 水 为溶剂， 反应 8.0h， 以52%的产率得到pyrrole-2-carboxylate
  参考文献：
  名称：

  Microbial synthesis of pyrrole-2-car☐ylate by Bacillus megaterium PYR2910

  摘要：

  Pyrrole-2-carboxylate was synthesized from pyrrole using the carboxylation reaction of reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910. By addition of high amounts of bicarbonate, the reaction equilibrium was shifted towards pyrrole-2-carboxylate. (C) 1998 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4039(98)00718-7

文献信息

• Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910
  作者：Marco Wieser、Noriko Fujii、Toyokazu Yoshida、Toru Nagasawa

  DOI：10.1046/j.1432-1327.1998.2570495.x

  日期：1998.10.15

  Pyrrole‐2‐carboxylate decarboxylase from Bacillusmegaterium PYR2910 attains a balanced reaction equilibrium with an equilibrium constant of 0.3−0.4 M. Therefore, the enzyme catalyzes the reverse carboxylation of pyrrole after addition of bicarbonate. For the synthesis of pyrrole‐2‐carboxylate, the reverse reaction was optimized and the equilibrium was shifted towards the carboxylate. The product yield was 230 mM (25.5 g/l) pyrrole‐2‐carboxylate from 300 mM pyrrole in a batch reaction and 325 mM (36.1 g/l) from 400 mM pyrrole in a fed‐batch reaction, using both whole cells and the purified enzyme in a pH 8.0 reaction mixture with bicarbonate saturation of 1.9 M. Kinetic studies indicated, that bicarbonate is the reactive species used by this carbon dioxide‐fixation enzyme.
• Hormann K.; Andreesen J.R., Biol Chem Hoppe Seyler, 1994, 0177-3593, 211-8
  作者：Hormann K.、Andreesen J.R.

  DOI：——

  日期：——
• Two-Component Flavin-dependent Pyrrole-2-carboxylate Monooxygenase from Rhodococcus Sp.
  作者：Dorit Becker、Thomas Schrader、Jan R. Andreesen

  DOI：10.1111/j.1432-1033.1997.t01-1-00739.x

  日期：1997.11

  Pyrrole‐2‐carboxylate can serve as the sole source of carbon, nitrogen, and energy for a strain tentatively identified to belong to the genus Rhodococcus. An NADH‐dependent oxygenase activity was detected in cell extracts that initiated the degradation of the substrate. During purification of the enzyme, this activity was separated into two protein components which were both purified to apparent homogeneity. A small monomeric 18.7‐kDa protein designated as reductase, catalyzed in vitro the NADH and FAD‐dependent reduction of cytochrome c and had an NADH‐oxidase activity. The second component, a 54‐kDa protein with a trimeric native structure had no enzymatic activity by itself, but exhibited a pyrrole‐2‐carboxylate‐dependent oxygen consumption when it was complemented with the reductase component, FAD, and NADH. This indicated that the large protein referred to as oxygenase was responsible for the oxygen‐dependent hydroxylation of the substrate. The rate of an uncoupled NADH oxidation without hydroxylation of the substrate was found to be strongly dependent on the molar ratio of both components. The uncoupling was nearly completely suppressed by a 5–7‐fold molar excess of the oxygenase component. The small protein was N‐terminally blocked. It was thus proteolytically digested and four of the resulting peptides were sequenced comprising 47 amino acids. The sequences of these fragments were similar to the sequences reported for the small component of different two‐component flavin monooxygenases. Furthermore, the N‐terminus of the oxygenase component showed high sequence similarity to the second, usually large subunit of these enzymes and to two single‐component flavin monooxygenases. Thus, the enzyme from Rhodococcus sp. designated as pyrrole‐2‐carboxylate monooxygenase belongs to the recently discovered new class of two‐component flavin aromatic monooxygenases. Some of the basic properties of both components were determined and their interaction during catalysis was investigated.
• Novel continuous carboxylation using pressurized carbon dioxide by immobilized decarboxylase
  作者：Tomoko Matsuda、Ryo Marukado、Shinichi Koguchi、Toru Nagasawa、Masaharu Mukouyama、Tadao Harada、Kaoru Nakamura

  DOI：10.1016/j.tetlet.2008.08.004

  日期：2008.10

  Novel continuous flow carboxylation system was constructed using pressurized CO2 at 6.5 MPa and immobilized enzyme, Bacillus megaterium PYR 2910 decarboxylase. The decarboxylase catalyzed the backward reaction, carboxylation, to convert pyrrole to pyrrole-2-carboxylate at the improved space-time yield by 25 times compared to the corresponding batch reaction. (C) 2008 Elsevier Ltd. All rights reserved.
• Microbial synthesis of pyrrole-2-car☐ylate by Bacillus megaterium PYR2910
  作者：Marco Wieser、Toyokazu Yoshida、Toru Nagasawa

  DOI：10.1016/s0040-4039(98)00718-7

  日期：1998.6

  Pyrrole-2-carboxylate was synthesized from pyrrole using the carboxylation reaction of reversible pyrrole-2-carboxylate decarboxylase from Bacillus megaterium PYR2910. By addition of high amounts of bicarbonate, the reaction equilibrium was shifted towards pyrrole-2-carboxylate. (C) 1998 Elsevier Science Ltd. All rights reserved.