(6R)-6-lactoyl-5,6,7,8-tetrahydropterin

• 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: (6R)-6-lactoyl-5,6,7,8-tetrahydropterin
• 英文别名: (6R)-2-amino-6-(2-hydroxypropanoyl)-5,6,7,8-tetrahydro-3H-pteridin-4-one
• 化学式: C₉H₁₃N₅O₃
• 分子量: 239.23
• InChiKey: HKCYZTKHPLJZDR-SRBOSORUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.6
• 重原子数：
  17
• 可旋转键数：
  2
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  129
• 氢给体数：
  5
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (6R)-6-lactoyl-5,6,7,8-tetrahydropterin 、 NADP⁺ 生成 1-[(6R)-2-amino-4-oxo-5,6,7,8-tetrahydro-1H-pteridin-6-yl]propane-1,2-dione 、 氢(+1)阳离子 、 NADPH(4-)
  参考文献：
  名称：

  四氢生物蝶呤的生物合成：将二氢蝶呤三磷酸转化为四氢蝶呤中间体。

  摘要：

  已知从GTP从头合成四氢生物蝶呤的第一步是将GTP转化为二氢蝶呤三磷酸。最新证据支持以下结论：在第一步之外，该途径中的蝶呤中间体均处于还原的四氢水平。现在我们已经表明，从大鼠肝脏，大鼠大脑和牛肾上腺髓质中部分纯化的馏分催化二氢蝶呤三磷酸转化为四氢生物蝶呤，以及途径中的假定中间体6-丙酮酰基-四氢蝶呤和6-乳酰基-四氢蝶呤。酶和化学研究的结果均支持后两种四氢蝶呤的指定结构。我们还从大脑中广泛纯化了一种不同于Sepaapterin还原酶的酶，催化依赖于TPNH的6-丙酮酰四氢蝶呤还原为6-乳糖基-四氢蝶呤。该还原酶在四氢生物蝶呤合成中的作用尚未确定。

  DOI：

  10.1016/0006-291x(85)91053-8
• 作为产物：
  描述：

  (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin 、 NADP⁺ 生成 (6R)-6-lactoyl-5,6,7,8-tetrahydropterin 、 氢(+1)阳离子 、 NADPH(4-)
  参考文献：
  名称：

  Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II

  摘要：

  Sepiapterin reductase (SPR) catalyzes the last step in the pathway of tetrahydrobiopterin biosynthesis in tissues. SPR is phosphorylated by Ca2+-dependent protein kinases, which indicates that Ca2+-activated protein kinases may play a role in the regulation of SPR in vivo. Phosphorylation sites of rat sepiapterin reductase (rSPR) by Ca2+/calmodulin-dependent protein kinase II were determined in the present study. Using specific monoclonal anti-phospho-Ser and -Thr antibodies, we found that only Ser residues of rSPR were phosphorylated. We constructed several point mutants of SPR by systematically replacing the three Ser residues by Ala ones. These mutants showed that all three Ser residues, i.e. S46, S196, and S214, of rSPR were phosphorylated. We also recognized that only Ser-213 of human SPR was phosphorylated. Each of these serine residues in SPR was found in the consensus sequence (Arg-X-X-Ser/Thr) of the phosphorylation site. (C) 2002 Elsevier Science B.V. All rights reserved.

  DOI：

  10.1016/s0167-4838(01)00300-4

文献信息

• Biosynthesis of tetrahydrobiopterin: Conversion of dihydroneopterin triphosphate to tetrahydropterin intermediates
  作者：S. Milstien、S. Kaufman

  DOI：10.1016/0006-291x(85)91053-8

  日期：1985.5

  synthesis of tetrahydrobiopterin from GTP is the conversion of GTP to dihydroneopterin triphosphate. Recent evidence supports the conclusion that beyond this first step, the pterin intermediates in the pathway are all at the tetrahydro level of reduction. We have now shown that partially purified fractions from rat liver, rat brain and bovine adrenal medulla catalyze the conversion of dihydroneopterin triphosphate

  已知从GTP从头合成四氢生物蝶呤的第一步是将GTP转化为二氢蝶呤三磷酸。最新证据支持以下结论：在第一步之外，该途径中的蝶呤中间体均处于还原的四氢水平。现在我们已经表明，从大鼠肝脏，大鼠大脑和牛肾上腺髓质中部分纯化的馏分催化二氢蝶呤三磷酸转化为四氢生物蝶呤，以及途径中的假定中间体6-丙酮酰基-四氢蝶呤和6-乳酰基-四氢蝶呤。酶和化学研究的结果均支持后两种四氢蝶呤的指定结构。我们还从大脑中广泛纯化了一种不同于Sepaapterin还原酶的酶，催化依赖于TPNH的6-丙酮酰四氢蝶呤还原为6-乳糖基-四氢蝶呤。该还原酶在四氢生物蝶呤合成中的作用尚未确定。
• Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II
  作者：Kengo Fujimoto、Susumu Y. Takahashi、Setsuko Katoh

  DOI：10.1016/s0167-4838(01)00300-4

  日期：2002.1

  Sepiapterin reductase (SPR) catalyzes the last step in the pathway of tetrahydrobiopterin biosynthesis in tissues. SPR is phosphorylated by Ca2+-dependent protein kinases, which indicates that Ca2+-activated protein kinases may play a role in the regulation of SPR in vivo. Phosphorylation sites of rat sepiapterin reductase (rSPR) by Ca2+/calmodulin-dependent protein kinase II were determined in the present study. Using specific monoclonal anti-phospho-Ser and -Thr antibodies, we found that only Ser residues of rSPR were phosphorylated. We constructed several point mutants of SPR by systematically replacing the three Ser residues by Ala ones. These mutants showed that all three Ser residues, i.e. S46, S196, and S214, of rSPR were phosphorylated. We also recognized that only Ser-213 of human SPR was phosphorylated. Each of these serine residues in SPR was found in the consensus sequence (Arg-X-X-Ser/Thr) of the phosphorylation site. (C) 2002 Elsevier Science B.V. All rights reserved.