2-Iminopropionsaeure | 3125-84-6

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: 2-Iminopropionsaeure
• 英文别名: 2-iminopropanoic acid；2-Iminiopropanoate
• CAS: 3125-84-6
• 化学式: C₃H₅NO₂
• mdl: MFCD19229044
• 分子量: 87.0782
• InChiKey: DUAWRLXHCUAWMK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  6
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.333
• 拓扑面积：
  61.2
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-Iminopropionsaeure 在 水 作用下， 生成 丙酮酸
  参考文献：
  名称：

  离子液体作为酶促合成的性能添加剂

  摘要：

  电化学合成将氧化还原酶催化的反应与电化学反应物的供应结合起来。使用离子液体作为性能添加剂可有助于克服这些合成方法的现有局限性。在这里，我们报告了三种典型的电酶合成过程中不同水溶性离子液体对电导率，生物催化剂活性，稳定性或底物溶解度等关键参数的影响。在这些研究中，确定了有前途的离子液体，并已用作制备规模的三种电解体系的批量电解的添加剂。可以将NADPH的电化学再生的时空产率提高三倍。对于氨基酸氧化酶催化的蛋氨酸消旋体的拆分，以及二茂铁介导的酶结合辅因子FAD的电化学再生，可实现时空产率提高50％，催化剂利用率（TTN）提高140％。此外，对于氯过氧化物酶催化的（R）-苯基甲基亚砜通过电化学生成所需的共底物H 2 O 2，根据所使用的离子液体的不同，时空产率和催化剂利用率可提高至4.2倍。

  DOI：

  10.1002/chem.200901046
• 作为产物：
  描述：

  2-氨基-2-丙烯酸 生成 2-Iminopropionsaeure
  参考文献：
  名称：

  Crystal Structure of Serine Dehydratase from Rat Liver^,

  摘要：

  SDH (L-serine dehydratase, EC 4.3.1.17) catalyzes the pyridoxal 5'-phosphate (PLP)-dependent dehydration of L-serine to yield pyruvate and ammonia. Liver SDH plays an important role in gluconeogenesis. Formation of pyruvate by SDH is a two-step reaction in which the hydroxyl group of serine is cleaved to produce aminoacrylate, and then the aminoacrylate is deaminated by nonenzymatic hydrolysis to produce pyruvate. The crystal structure of rat liver apo-SDH was determined by single isomorphous replacement at 2.8 A resolution. The holo-SDH crystallized with O-methylserine (OMS) was also determined at 2.6 A resolution by molecular replacement. SDH is composed of two domains, and each domain has a typical alphabeta-open structure. The active site is located in the cleft between the two domains. The holo-SDH contained PLP-OMS aldimine in the active site, indicating that OMS can form the Schiff base linkage with PLP, but the subsequent dehydration did not occur. Apo-SDH forms a dimer by inserting the small domain into the catalytic cleft of the partner subunit so that the active site is closed. Holo-SDH also forms a dimer by making contacts at the back of the clefts so that the dimerization does not close the catalytic cleft. The phosphate group of PLP is surrounded by a characteristic G-rich sequence ((168)GGGGL(172)) and forms hydrogen bonds with the amide groups of those amino acid residues, suggesting that the phosphate group can be protonated. N(1) of PLP participates in a hydrogen bond with Cys303, and similar hydrogen bonds with N(1) participating are seen in other beta-elimination enzymes. These hydrogen bonding schemes indicate that N(1) is not protonated, and thus, the pyridine ring cannot take a quinone-like structure. These characteristics of the bound PLP suggest that SDH catalysis is not facilitated by forming the resonance-stabilized structure of the PLP-Ser aldimine as seen in aminotransferases. A possible catalytic mechanism involves the phosphate group, surrounded by the characteristic sequence, acting as a general acid to donate a proton to the leaving hydroxyl group of serine.

  DOI：

  10.1021/bi035324p

文献信息

• Favero, 1953, vol. <8> 14, p. 433,520, 525
  作者：Favero

  DOI：——

  日期：——
• Conserved YjgF Protein Family Deaminates Reactive Enamine/Imine Intermediates of Pyridoxal 5′-Phosphate (PLP)-dependent Enzyme Reactions
  作者：Jennifer A. Lambrecht、Jeffrey M. Flynn、Diana M. Downs

  DOI：10.1074/jbc.m111.304477

  日期：2012.1

  The YjgF/YER057c/UK114 family of proteins is conserved in all domains of life, suggesting that the role of these proteins arose early and was maintained throughout evolution. Metabolic consequences of lacking this protein in Salmonella enterica and other organisms have been described, but the biochemical function of YjgF remained unknown. This work provides the first description of a conserved biochemical activity for the YjgF protein family. Our data support the conclusion that YjgF proteins have enamine/imine deaminase activity and accelerate the release of ammonia from reactive enamine/imine intermediates of the pyridoxal 5'-phosphate-dependent threonine dehydratase (IlvA). Results from structure-guided mutagenesis experiments suggest that YjgF lacks a catalytic residue and that it facilitates ammonia release by positioning a critical water molecule in the active site. YjgF is renamed RidA (reactive intermediate/imine deaminase A) to reflect the conserved activity of the protein family described here. This study, combined with previous physiological studies on yjgF mutants, suggests that intermediates of pyridoxal 5'-phosphate-mediated reactions may have metabolic consequences in vivo that were previously unappreciated. The conservation of the RidA/YjgF family suggests that reactive enamine/imine metabolites are of concern to all organisms.
• l-serine dehydrataste from rat liver. Purification and some properties
  作者：Dietrich Simon、Jiro Hoshino、Hans Kröger

  DOI：10.1016/0005-2744(73)90091-0

  日期：1973.9
• Bacterial l-serine dehydratases: a new family of enzymes containing iron-sulfur clusters
  作者：Reiner Grabowski、Antje E.M. Hofmeister、Wolfgang Buckel

  DOI：10.1016/0968-0004(93)90040-t

  日期：1993.8

  Two families of enzymes are described which catalyse identical chemical reactions but differ in their prosthetic groups and hence in their mechanism of action. One family, the pyridoxal-5'-phosphate (PLP)-dependent L-threonine dehydratases, also use L-serine as substrate. The other, hitherto unrecognized family is the iron-dependent, highly specific bacterial L-serine dehydratases. It has been shown that L-serine dehydratase from the anaerobic bacterium Peptostreptococcus asaccharolyticus contains an iron-sulfur cluster but no PLP. A mechanism for the dehydration of L-serine which is similar, but not identical, to that of the dehydration of citrate catalysed by aconitase is proposed.
• Ionic Liquids as Performance Additives for Electroenzymatic Syntheses
  作者：Christina Kohlmann、Lasse Greiner、Walter Leitner、Christian Wandrey、Stephan Lütz

  DOI：10.1002/chem.200901046

  日期：2009.11.2

  Electroenzymatic syntheses combine oxidoreductase‐catalysed reactions with electrochemical reactant supply. The use of ionic liquids as performance additives can contribute to overcoming existing limitations of these syntheses. Here, we report on the influence of different water‐miscible ionic liquids on critical parameters such as conductivity, biocatalyst activity and stability or substrate solubility

  电化学合成将氧化还原酶催化的反应与电化学反应物的供应结合起来。使用离子液体作为性能添加剂可有助于克服这些合成方法的现有局限性。在这里，我们报告了三种典型的电酶合成过程中不同水溶性离子液体对电导率，生物催化剂活性，稳定性或底物溶解度等关键参数的影响。在这些研究中，确定了有前途的离子液体，并已用作制备规模的三种电解体系的批量电解的添加剂。可以将NADPH的电化学再生的时空产率提高三倍。对于氨基酸氧化酶催化的蛋氨酸消旋体的拆分，以及二茂铁介导的酶结合辅因子FAD的电化学再生，可实现时空产率提高50％，催化剂利用率（TTN）提高140％。此外，对于氯过氧化物酶催化的（R）-苯基甲基亚砜通过电化学生成所需的共底物H 2 O 2，根据所使用的离子液体的不同，时空产率和催化剂利用率可提高至4.2倍。