氨基甲酰磷酸 | 590-55-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 中文名称: 氨基甲酰磷酸
• 中文别名: 胺甲醯膦酸
• 英文名称: carbamoyl phosphate
• 英文别名: Carbamoylphosphate；carbamyl phosphate；carbamoyl-phosphate；Carbamoyl-phosphorsaeure；Carbamoylphosphorsaeure；phosphono carbamate
• CAS: 590-55-6
• 化学式: CH₄NO₅P
• 分子量: 141.02
• InChiKey: FFQKYPRQEYGKAF-UHFFFAOYSA-N

物化性质

• 沸点：
  403.3±28.0 °C(Predicted)
• 密度：
  1.976±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -2.1
• 重原子数：
  8
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  110
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  氨基甲酰磷酸 在 aspartate transcarbamylase (ATCase) 作用下， 反应 24.0h， 生成 二氧化碳 、 alkaline earth salt of/the/ methylsulfuric acid
  参考文献：
  名称：

  Waldrop, Grover L.; Urbauer, Jeffrey L.; Cleland, Journal of the American Chemical Society, 1992, vol. 114, # 15, p. 5941 - 5945

  摘要：

  DOI：
• 作为产物：
  描述：

  potassium hydrogencarbonate 在 L-鸟氨酸 、 L-谷氨酰胺 、 potassium chloride 、 5’-三磷酸腺苷 、 magnesium chloride 作用下， 生成 氨基甲酰磷酸
  参考文献：
  名称：

  Carbamate Transport in Carbamoyl Phosphate Synthetase: A Theoretical and Experimental Investigation

  摘要：

  The transport of carbamate through the large subunit of carbamoyl phosphate synthetase (CPS) from Escherichia coli was investigated by molecular dynamics and site-directed mutagenesis. Carbamate, the product of the reaction involving ATP, bicarbonate, and ammonia, must be delivered from the site of formation to the site of utilization by traveling nearly 40 angstrom within the enzyme. Potentials of mean force (PMF) calculations along the entire tunnel for the translocation of carbamate indicate that the tunnel is composed of three continuous water pockets and two narrow connecting parts, near Ala-23 and Gly-575. The two narrow parts render two free energy barriers of 6.7 and 8.4 kcal/mol, respectively. Three water pockets were filled with about 21, 9, and 9 waters, respectively, and the corresponding relative free energies of carbamate residing in these free energy minima are 5.8, 0, and 1.6 kcal/mol, respectively. The release of phosphate into solution at the site for the formation of carbamate allows the side chain of Arg-306 to rotate toward Glu-25, Glu-383, and Glu-604. This rotation is virtually prohibited by a barrier of at least 23 kcal/mol when phosphate remains bound. This conformational change not only opens the entrance of the tunnel but also shields the charge-charge repulsion from the three glutamate residues when carbamate passes through the tunnel. Two mutants, A23F and G575F, were designed to block the migration of carbamate through the narrowest parts of the carbamate tunnel. The mutants retained only 1.7% and 3.8% of the catalytic activity for the synthesis of carbamoyl phosphate relative to the wild type CPS, respectively.

  DOI：

  10.1021/ja910441v
• 作为试剂：
  描述：

  二磷酸腺苷 在 glucose-6-phosphate dehydrogenase 、 L-鸟氨酸 、 葡萄糖 、 氨基甲酰磷酸 、 potassium chloride 、 β-烟酰胺腺嘌呤二核苷酸 、 magnesium chloride 、 hexokinase 作用下， 生成 5’-三磷酸腺苷
  参考文献：
  名称：

  Carbamate Transport in Carbamoyl Phosphate Synthetase: A Theoretical and Experimental Investigation

  摘要：

  The transport of carbamate through the large subunit of carbamoyl phosphate synthetase (CPS) from Escherichia coli was investigated by molecular dynamics and site-directed mutagenesis. Carbamate, the product of the reaction involving ATP, bicarbonate, and ammonia, must be delivered from the site of formation to the site of utilization by traveling nearly 40 angstrom within the enzyme. Potentials of mean force (PMF) calculations along the entire tunnel for the translocation of carbamate indicate that the tunnel is composed of three continuous water pockets and two narrow connecting parts, near Ala-23 and Gly-575. The two narrow parts render two free energy barriers of 6.7 and 8.4 kcal/mol, respectively. Three water pockets were filled with about 21, 9, and 9 waters, respectively, and the corresponding relative free energies of carbamate residing in these free energy minima are 5.8, 0, and 1.6 kcal/mol, respectively. The release of phosphate into solution at the site for the formation of carbamate allows the side chain of Arg-306 to rotate toward Glu-25, Glu-383, and Glu-604. This rotation is virtually prohibited by a barrier of at least 23 kcal/mol when phosphate remains bound. This conformational change not only opens the entrance of the tunnel but also shields the charge-charge repulsion from the three glutamate residues when carbamate passes through the tunnel. Two mutants, A23F and G575F, were designed to block the migration of carbamate through the narrowest parts of the carbamate tunnel. The mutants retained only 1.7% and 3.8% of the catalytic activity for the synthesis of carbamoyl phosphate relative to the wild type CPS, respectively.

  DOI：

  10.1021/ja910441v

文献信息

• Characterization of NovP and NovN: Completion of Novobiocin Biosynthesis by Sequential Tailoring of the Noviosyl Ring
  作者：Caren L. Freel Meyers、Markus Oberthür、Hui Xu、Lutz Heide、Daniel Kahne、Christopher T. Walsh

  DOI：10.1002/anie.200352626

  日期：2004.1
• Gmelin Handbuch der Anorganischen Chemie, Gmelin Handbook: C: MVol.D1, 44, page 387 - 389
  作者：

  DOI：——

  日期：——
• N-Carbamoylation of 2,4-Diaminobutyrate Reroutes the Outcome in Padanamide Biosynthesis
  作者：Yi-Ling Du、Doralyn S. Dalisay、Raymond J. Andersen、Katherine S. Ryan

  DOI：10.1016/j.chembiol.2013.06.013

  日期：2013.8

  Padanamides are linear tetrapeptides notable for the absence of proteinogenic amino acids in their structures. In particular, two unusual heterocycles, (S)-3-amino-2,-oxopyrrolidine-1-carboxamide (S-Aopc) and (S)-3-aminopiperidine-2,6-dione (S-Apd), are found at the C-termini of padanamides A and B, respectively. Here we identify the padanamide biosynthetic gene cluster and carry out systematic gene inactivation studies. Our results show that padanamides are synthesized by highly dissociated hybrid nonribosomal peptide synthetase/polyketide synthase machinery. We further demonstrate that carbamoyltransferase gene padQ is critical to the formation of padanamide A but dispensable for biosynthesis of padanamide B. Biochemical investigations show that PadQ carbamoylates the rare biosynthetic precursor L-2,4-diaminobutyrate, generating L-2-amino-4-ureidobutyrate, the presumed precursor to the C-terminal residue of padanamide A. By contrast, the C-terminal residue of padanamide B may derive from glutamine. An unusual thioesterase-catalyzed cyclization is proposed to generate the S-Aopc/S-Apd heterocycles.
• Halmann, M.; Lapidot, A.; Samuel, D., Journal of the Chemical Society
  作者：Halmann, M.、Lapidot, A.、Samuel, D.

  DOI：——

  日期：——