2-氨基-6-甲基-6,7-二氢-4(1H)-蝶啶酮 | 98482-90-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 蝶啶及其衍生物
• 中文名称: 2-氨基-6-甲基-6,7-二氢-4(1H)-蝶啶酮
• 中文别名: 4-噻唑甲胺,2-(2-氯苯基)-
• 英文名称: 6-methyl-5,6,7,8-tetrahydropterin
• 英文别名: 6-methyldihydro-(6H)-pterin；2-amino-6-methyl-6,7-dihydro-3H-pteridin-4-one
• CAS: 98482-90-7
• 化学式: C₇H₉N₅O
• 分子量: 179.181
• InChiKey: QARNTSWBYSPKTL-UHFFFAOYSA-N

物化性质

• 密度：
  1.78±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  13
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  92.2
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-氨基-6-甲基-6,7-二氢-4(1H)-蝶啶酮 在 1,4-dihydronicotinamide adenine dinucleotide 、 dihydropteridine reductase 、 双氧水 作用下， 以 various solvent(s) 为溶剂， 生成 2-氨基-7,8-二氢-6-甲基-4(1H)-蝶啶酮
  参考文献：
  名称：

  The dihydropteridine reductase (human brain) activity of some lipophilic quinonoid dihydropterins

  摘要：

  DOI：

  10.1016/0223-5234(87)90001-8
• 作为产物：
  描述：

  2-氨基-6-甲基-5,6,7,8-四氢蝶啶-4(1H)-酮 在 盐酸 、 E₃₃₂A tyrosine hydroxylase 、 L-酪氨酸 、 氯化铵 、 ethylenediamine Tetraacetic Acid 作用下， 以 甲醇 、 水 为溶剂， 生成 2-氨基-6-甲基-6,7-二氢-4(1H)-蝶啶酮
  参考文献：
  名称：

  Characterization of Unstable Products of Flavin- and Pterin-Dependent Enzymes by Continuous-Flow Mass Spectrometry

  摘要：

  Continuous-flow mass spectrometry (CFMS) was used to monitor the products formed during the initial 2 0.25-20 s of the reactions catalyzed by the flavoprotein N-acetylpolyamine oxidase (PAO) and the pterin-dependent enzymes phenylalanine hydroxylase (PheH) and tyrosine hydroxylase (TyrH). N,N'-Dibenzyl-1,4-diaminobutane (DBDB) is a substrate for PAO for which amine oxidation is rate-limiting. CFMS of the reaction showed formation of an initial imine due to oxidation of an exo-carbon-nitrogen bond. Nonenzymatic hydrolysis of the imine formed benzaldehyde and N-benzyl-1,4-diaminobutane; the subsequent oxidation by PAO of the latter to an additional imine could also be followed. Measurement of the deuterium kinetic isotope effect on DBDB oxidation by CFMS yielded a value of 7.6 +/- 0.3, in good agreement with a value of 6.7 +/- 0.6 from steady-state kinetic analyses. In the PheH reaction, the transient formation of the 4a-hydroxypterin product was readily detected; tandem mass spectrometry confirmed attachment of the oxygen to C(4a). With wild-type TyrH, the 4a-hydroxypterin was also the product. In contrast, no product other than a dihydropterin could be detected in the reaction of the mutant protein E332A TyrH.

  DOI：

  10.1021/bi500267c

文献信息

• The Synthesis of 6-Aminomethyl-5,6,7,8-Tetrahydropterin
  作者：P Waring

  DOI：10.1071/ch9880667

  日期：——

  6-Aminomethyl-5,6,7,8-tetrahydropterin has been prepared by reduction of 2-acetamido-6-cyanopteridin-4(3H)-one* to 2-acetamido-6-aminomethyl- 5,6,7,8-tetrahydropteridin-4(3H)-one followed by acid hydrolysis. The hitherto undescribed 6-cyanopterin was prepared by careful hydrolysis of the 2-acetamido compound prepared by dehydration of the oxime derived from 2-acetamido-6-formylpteridin-4(3H)-one. The latter was prepared by selenium dioxide oxidation of the methyl compound. Oxidation of 6-aminomethyl-5,6,7,8-tetrahydropterin at neutral pH appears to proceed with significant side-chain loss in Tris buffer but not in phosphate buffer.

  通过将 2-乙酰氨基-6-氰基蝶啶-4(3H)-酮*还原为 2-乙酰氨基-6-氨基甲基-5,6,7,8-四氢蝶啶-4(3H)-酮，然后进行酸水解，制备出了 6-氨基甲基-5,6,7,8-四氢蝶啶。通过对 2-乙酰氨基-6-甲酰基蝶啶-4(3H)-酮肟脱水制备的 2-乙酰氨基化合物进行仔细水解，制备出了迄今为止尚未发现的 6-氰基蝶呤。后者是通过二氧化硒氧化甲基化合物制备的。在中性 pH 值下，6-氨甲基-5,6,7,8-四氢蝶呤的氧化似乎是在三羟甲基丙烷缓冲液中进行的，但在磷酸盐缓冲液中侧链损失不大。
• MATSUURA, SADAO;MURATA, SHIZUAKI;SUGIMOTO, TAKASHI, CHEM. AND BIOL. PTERIDINES, 1986. PTERIDINES AND FOLIC ACID DERIV. PROC. +
  作者：MATSUURA, SADAO、MURATA, SHIZUAKI、SUGIMOTO, TAKASHI

  DOI：——

  日期：——
• The dihydropteridine reductase (human brain) activity of some lipophilic quinonoid dihydropterins
  作者：Paul Waring、Wilfred L.F Armarego

  DOI：10.1016/0223-5234(87)90001-8

  日期：1987.3
• Characterization of Unstable Products of Flavin- and Pterin-Dependent Enzymes by Continuous-Flow Mass Spectrometry
  作者：Kenneth M. Roberts、José R. Tormos、Paul F. Fitzpatrick

  DOI：10.1021/bi500267c

  日期：2014.4.29

  Continuous-flow mass spectrometry (CFMS) was used to monitor the products formed during the initial 2 0.25-20 s of the reactions catalyzed by the flavoprotein N-acetylpolyamine oxidase (PAO) and the pterin-dependent enzymes phenylalanine hydroxylase (PheH) and tyrosine hydroxylase (TyrH). N,N'-Dibenzyl-1,4-diaminobutane (DBDB) is a substrate for PAO for which amine oxidation is rate-limiting. CFMS of the reaction showed formation of an initial imine due to oxidation of an exo-carbon-nitrogen bond. Nonenzymatic hydrolysis of the imine formed benzaldehyde and N-benzyl-1,4-diaminobutane; the subsequent oxidation by PAO of the latter to an additional imine could also be followed. Measurement of the deuterium kinetic isotope effect on DBDB oxidation by CFMS yielded a value of 7.6 +/- 0.3, in good agreement with a value of 6.7 +/- 0.6 from steady-state kinetic analyses. In the PheH reaction, the transient formation of the 4a-hydroxypterin product was readily detected; tandem mass spectrometry confirmed attachment of the oxygen to C(4a). With wild-type TyrH, the 4a-hydroxypterin was also the product. In contrast, no product other than a dihydropterin could be detected in the reaction of the mutant protein E332A TyrH.