6,7-Dihydropteridine

• 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
• 英文名称: 6,7-Dihydropteridine
• 化学式: C₆H₆N₄
• 分子量: 134.14
• InChiKey: KVDQMARGGBLIJM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.9
• 重原子数：
  10
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  49.4
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  5,6,7,8-四氢-蝶啶 、 NADP⁺ 生成 6,7-Dihydropteridine 、 氢(+1)阳离子 、 NADPH(4-)
  参考文献：
  名称：

  来自牛肝的二氢蝶呤还原酶。与NADH的二元复合物的纯化，结晶和分离。

  摘要：

  从牛肝中纯化二氢蝶呤还原酶[EC 1.6.99.7]，产率为50％，并结晶。纯化的酶的理化性质与绵羊肝二氢蝶呤还原酶的理化性质非常相似。然而，在纯化过程中，通过在CM-Sephadex上进行柱色谱分析，发现该酶被分为2个主要峰和次要峰，其中一个主要峰被鉴定为该酶与NADH的二元复合物。还在体外制备了还原酶-NADH复合物并使其结晶。在将醌类-二氢蝶呤添加到复合物中后，NADH被氧化并从酶中释放。结合的NADH的量经计算为每摩尔还原酶2摩尔。还原酶-NADH的发生经计算为每摩尔还原酶2摩尔。牛肝提取物中以主要形式存在的还原酶-NADH复合物与作为辅酶的NADH的吡啶核苷酸特异性一致。结果进一步支持以下观点：NADH是该还原酶的天然辅酶。

  DOI：

  10.1093/oxfordjournals.jbchem.a131432

文献信息

• A New Enzyme, NADPH-Dihydropteridine Reductase in Bovine Liver
  作者：Nobuo NAKANISHI、Hiroyuki HASEGAWA、Shoji WATABE

  DOI：10.1093/oxfordjournals.jbchem.a131504

  日期：1977.3

  An enzyme designated as NADPH-dihydropteridine reductase was found in the extract of bovine liver and partially purified. In contrast to NADH-dependent dihydropteridine reductase [EC 1.6.99.7], the enzyme catalyzes the reduction of quinonoid-dihydropterin to tetrahydropterin the presence of NADPH. The two enzymes were separated by column chromatography on DEAE-Sephadex. Tyrosine formation in the phenylalanine hydroxylation system was also stimulated by NADPH-dihydropteridine reductase. The existence of these two dihydropteridine reductases suggests that the tetrahydro form of pteridine cofactor may be regenerated in two different ways in vivo.

  在牛肝提取物中发现了NADPH-二氢蝶啶还原酶，并对其进行了部分纯化。与NADH依赖性二氢蝶啶还原酶（EC 1.6.99.7）不同，该酶在NADPH存在的情况下催化醌二氢蝶啶还原为四氢蝶啶。通过DEAE-Sephadex柱层析法将这两种酶分离。苯丙氨酸羟化系统中的酪氨酸形成也受到NADPH-二氢蝶啶还原酶的刺激。这两种二氢蝶啶还原酶的存在表明，蝶啶辅因子的四氢形式可以在体内以两种不同的方式再生。
• Nucleobase editors and uses thereof
  申请人：President and Fellows of Harvard College

  公开号：US10167457B2

  公开（公告）日：2019-01-01

  Some aspects of this disclosure provide strategies, systems, reagents, methods, and kits that are useful for the targeted editing of nucleic acids, including editing a single site within the genome of a cell or subject, e.g., within the human genome. In some embodiments, fusion proteins of Cas9 and nucleic acid editing proteins or protein domains, e.g., deaminase domains, are provided. In some embodiments, methods for targeted nucleic acid editing are provided. In some embodiments, reagents and kits for the generation of targeted nucleic acid editing proteins, e.g., fusion proteins of Cas9 and nucleic acid editing proteins or domains, are provided.

  本公开的某些方面提供了用于核酸靶向编辑的策略、系统、试剂、方法和试剂盒，包括编辑细胞或受试者基因组内的单个位点，例如人类基因组内的单个位点。在一些实施方案中，提供了 Cas9 与核酸编辑蛋白或蛋白结构域（如脱氨酶结构域）的融合蛋白。在一些实施方案中，提供了用于靶向核酸编辑的方法。在一些实施方案中，提供了用于产生靶向核酸编辑蛋白（例如 Cas9 和核酸编辑蛋白或结构域的融合蛋白）的试剂和试剂盒。
• Dihydropteridine Reductase. Investigation of the Specificity for Quinoid Dihydropteridine and the Inhibition by 2,4-Diaminopteridines
  作者：Kirsten E. Lind

  DOI：10.1111/j.1432-1033.1972.tb01728.x

  日期：1972.2

  Dihydropteridine reductase, which catalyses the reduction of quinoid dihydropteridines in the presence of NADH or NADPH, has been purified approximately 800‐fold from rat liver tissue. The specificity of the purified dihydropteridine reductase with respect to quinoid dihydropteridine has been studied, by comparing the Michaelis constants and maximum velocity in systems containing the same concentration of enzyme. In addition, the inhibitory effect of some 2,4‐diaminopteridines has been studied. Furthermore the present work shows, that the quinone reductase activity observed with a previously used dihydropteridine reductase preparation is attributable to the presence of a quinone reductase in this preparation.
• POWDERED POUCH AND METHOD OF MAKING SAME
  申请人：Monosol, LLC

  公开号：EP2838811B1

  公开（公告）日：2018-06-06
• COMPOSITIONS AND METHODS FOR MODULATING METABOLIC REGULATORS OF T CELL PATHOGENICITY
  申请人：The Broad Institute, Inc.

  公开号：US20220142948A1

  公开（公告）日：2022-05-12

  The subject matter disclosed herein is generally directed to modulation of Th17 differentiation and pathogenicity by use of metabolic targets. The metabolic targets are the molecules of the polyamine pathway or glycolysis pathway. Modulation of the polyamine pathway can shift Th17 pathogenicity and shift the transcriptome of Th17 cells to a Treg or Th1 transcriptome. The polyamine analogue DFMO can be used to modulate an inflammatory response. Inhibitors of enzymes in the glycolysis pathway can shift Th17 pathogenicity.