[(3R)-piperidine-3-carbonyl]azanium

• 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: [(3R)-piperidine-3-carbonyl]azanium
• 化学式: C6H13N2O+
• 分子量: 129.18
• InChiKey: BVOCPVIXARZNQN-RXMQYKEDSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  9
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  59.7
• 氢给体数：
  2
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  [(3R)-piperidine-3-carbonyl]azanium 、 水 生成 (R)-(-)-哌啶-3-甲酸 、 铵
  参考文献：
  名称：

  A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide

  摘要：

  A novel amidase acting on (R,S)‐piperazine‐2‐tert‐butylcarboxamide was purified from Pseudomonas sp. MCI3434 and characterized. The enzyme acted R‐stereoselectively on (R,S)‐piperazine‐2‐tert‐butylcarboxamide to yield (R)‐piperazine‐2‐carboxylic acid, and was tentatively named R‐amidase. The N‐terminal amino acid sequence of the enzyme showed high sequence identity with that deduced from a gene named PA3598 encoding a hypothetical hydrolase in Pseudomonas aeruginosa PAO1. The gene encoding R‐amidase was cloned from the genomic DNA of Pseudomonas sp. MCI3434 and sequenced. Analysis of 1332 bp of the genomic DNA revealed the presence of one open reading frame (ramA) which encodes the R‐amidase. This enzyme, RamA, is composed of 274 amino acid residues (molecular mass, 30 128 Da), and the deduced amino acid sequence exhibits homology to a carbon–nitrogen hydrolase protein (PP3846) from Pseudomonas putida strain KT2440 (72.6% identity) and PA3598 protein from P. aeruginosa strain PAO1 (65.6% identity) and may be classified into a new subfamily in the carbon–nitrogen hydrolase family consisting of aliphatic amidase, β‐ureidopropionase, carbamylase, nitrilase, and so on. The amount of R‐amidase in the supernatant of the sonicated cell‐free extract of an Escherichia coli transformant overexpressing the ramA gene was about 30 000 times higher than that of Pseudomonas sp. MCI3434. The intact cells of the E. coli transformant could be used for the R‐stereoselective hydrolysis of racemic piperazine‐2‐tert‐butylcarboxamide. The recombinant enzyme was purified to electrophoretic homogeneity from cell‐free extract of the E. coli transformant overexpressing the ramA gene. On gel‐filtration chromatography, the enzyme appeared to be a monomer. It had maximal activity at 45 °C and pH 8.0, and was completely inactivated in the presence of p‐chloromercuribenzoate, N‐ethylmaleimide, Mn2+, Co2+, Ni2+, Cu2+, Zn2+, Ag+, Cd2+, Hg2+ or Pb2+. RamA had hydrolyzing activity toward the carboxamide compounds, in which amino or imino group is connected to β‐ or γ‐carbon, such as β‐alaninamide, (R)‐piperazine‐2‐carboxamide (R)‐piperidine‐3‐carboxamide, d‐glutaminamide and (R)‐piperazine‐2‐tert‐butylcarboxamide. The enzyme, however, did not act on the other amide substrates for the aliphatic amidase despite its sequence similarity to RamA.

  DOI：

  10.1111/j.1432-1033.2004.04069.x