α-glycerophosphate | 10030-38-3

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 甘油磷脂
• 英文名称: α-glycerophosphate
• 英文别名: sn-glycerol-1-phosphate；L-glycero-1-phosphate；(S)-glyceryl phosphate；Sn-glycerol 1-phosphate(2-)；[(2S)-2,3-dihydroxypropyl] phosphate
• CAS: 10030-38-3；10290-66-1；20445-96-9
• 化学式: C₃H₇O₆P
• 分子量: 170.059
• InChiKey: AWUCVROLDVIAJX-VKHMYHEASA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -3
• 重原子数：
  10
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  113
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  α-glycerophosphate 在 20 kU catalase 、 Eupergit C 250 L 、 L-α-glycerophosphate oxidase (EC 1.1.3.21 aus Pediococcus spec.) 作用下， 以 水 为溶剂， 反应 48.0h， 生成 1,3-dihydroxyacetone phosphate
  参考文献：
  名称：

  L-α-甘油磷酸氧化酶与过氧化氢酶的固定化及其在磷酸二羟丙酮合成中的应用

  摘要：

  在有氧条件下，通过与过氧化氢酶固定化的L-α-甘油磷酸氧化酶将L-α-甘油磷酸（1）氧化为磷酸二羟基丙酮（2），该酶用于分解生成的过氧化氢。2被困在与D / L-甘油醛的醛缩酶反应中（3）。共固定的酶显示出增加的操作稳定性，并且可以在进一步的转化中重复使用而不会丧失活性。

  DOI：

  10.1016/s0040-4020(97)01009-0
• 作为产物：
  描述：

  1,3-dihydroxyacetone phosphate 在 磷酸丙糖异构酶 、 3-磷酸甘油脱氢酶 、 还原型辅酶Ⅰ 作用下， 以 aq. buffer 为溶剂， 反应 0.17h， 生成 α-glycerophosphate
  参考文献：
  名称：

  l-Rhamnulose-1-phosphate and l-fuculose-1-phosphate aldolase mediated multi-enzyme cascade systems for nitrocyclitol synthesis

  摘要：

  One-pot multistep stereoselective cascade reactions were implemented for the straightforward synthesis of various nitrocyclitols. Two kinases, an aldolase and a phosphatase were involved in this process, together with a spontaneous intramolecular Henry reaction to provide the nitrocyclitol moiety. The C-C bond formation catalysed by the aldolase and the nitroaldol reactions were key steps to build the carbocycle stereoselectively. The aldolase acceptor substrates were all 4-nitrobutanal structurally based, either hydroxylated or unsubstituted at the C2 and/or C3 positions. L-Fuculose-1-phosphate aldolase (FucA) catalysed the formation of the expected (R,R)- or D-erythro aldol, except in the case of 4-nitrobutanal, from which the epimeric (R,S)- or L-threo aldol was also formed. L-Rhamnulose-1-phosphate aldolase consistently formed the expected (R,S)- or L-threo aldol together with a minor amount of (R,R)- or D-elythro aldol. The intramolecular Henry reaction was also found to be stereoselective, occurring spontaneously once the aldol was formed due to the presence of both ketone and a terminally positioned nitro group. The combination of this set of reactions successfully furnished 11 nitrocyclitols which have not been described previously in the literature. (C) 2014 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2014.10.016

文献信息

• (S)-2,3-Di-O-geranylgeranylglyceryl Phosphate Synthase from the Thermoacidophilic Archaeon Sulfolobus solfataricus
  作者：Hisashi Hemmi、Kyohei Shibuya、Yoshihiro Takahashi、Toru Nakayama、Tokuzo Nishino

  DOI：10.1074/jbc.m409207200

  日期：2004.11

  in almost all archaeal genomes clearly indicates the importance of their functions. A phylogenetic tree constructed using the amino acid sequences of some typical members of the UbiA prenyltransferase family and their homologues from suggests that the two other homologues, excluding the ()-2,3-di--geranylgeranylglyceryl phosphate synthase, are involved in the production of respiratory quinone and heme

  古细菌的膜脂的核心结构具有一些独特的特性，可以使古细菌与其他细菌，真核生物区别开来。（S）-2,3-二-O-香叶基香叶酸甘油酯磷酸合酶催化古兰基香叶基基团从香叶基香叶基二磷酸酯向（S）-3-O-香叶基香叶酸甘油酯磷酸酯的转移，参与古细菌膜脂质的生物合成。众所周知，在呼吸醌，血红素，叶绿素，维生素E和紫草素的生物合成中，UbiA异戊二烯基转移酶家族的酶催化异戊二烯基向具有疏水环结构的各种受体的转移。发现嗜热古细菌Sulfolobus solfataricus在其基因组中编码UbiA异戊二烯基转移酶的三个同源物。由SSO0583编码的同系物之一在大肠杆菌中表达，纯化和鉴定。放射分析和质谱分析数据表明该酶特异性催化（S）-2，3-二-O-香叶基香叶基甘油基磷酸酯的生物合成。该酶的直向同源物几乎在所有古细菌基因组中都编码，这一事实清楚地表明了其功能的重要性。使用UbiA异戊二烯基转移酶家族的一些典型成员的氨基酸序列及其来自S
• Purification and Properties of sn-Glycerol-1 -Phosphate Dehydrogenase from Methanobacterium thermoautotrophicum: Characterization of the Biosynthetic Enzyme for the Enantiomeric Glycerophosphate Backbone of Ether Polar Lipids of Archaea
  作者：M. Nishihara、Y. Koga

  DOI：10.1093/oxfordjournals.jbchem.a021791

  日期：1997.9.1

  enzyme which seems to be responsible for the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids was purified from a methanogenic archaeon, Methanobacterium thermoautotrophicum, and characterized. The enzyme, sn-glycerol-1-phosphate: NAD(P)+ oxidoreductase (sn-glycerol-1-phosphate dehydrogenase), was purified 7,600-fold from a cell

  从产甲烷的古细菌，嗜热自养甲烷杆菌中纯化出似乎对古细菌醚脂质的甘油磷酸骨架（sn-甘油-1-磷酸）的对映体构型负责的酶，并对其进行了表征。sn-甘油-1-磷酸酶：NAD（P）+氧化还原酶（sn-甘油-1-磷酸脱氢酶）通过硫酸铵分级分离和七个色谱步骤从无细胞提取物中纯化7600倍。在十二烷基硫酸钠存在下，最终制备物表现出的比活为617微摩尔/分钟/毫克（Vmax），并在聚丙烯酰胺凝胶电泳上产生对应于38kDa的单条带。天然酶在凝胶过滤色谱法上显示出302 kDa的表观分子量，表明它以同八聚体形式存在。在接近中性pH的75摄氏度下观察到最大活性。该活性被钾离子刺激。磷酸二羟基丙酮的Km比磷酸Sn-甘油-1-酯的Km小7.5倍，这表明Sn-甘油-1-磷酸酯的形成是细胞中的自然方向。在使用的测定条件下，未观察到产物抑制。确定了N末端氨基酸序列。
• Active site of Zn²⁺-dependent<i>sn</i>-glycerol-1-phosphate dehydrogenase from<i>Aeropyrum pernix</i>K1
  作者：Jin-Suk Han、Kazuhiko Ishikawa

  DOI：10.1155/2005/257264

  日期：——

  The enzymesn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) is key to the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. This enzyme catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate. To date, no information about the active site and catalytic mechanism of this enzyme has been reported. Using the sequence and structural information for glycerol dehydrogenase, we constructed six mutants (D144N, D144A, D191N, H271A, H287A and D191N/H271A) of Gro1PDH fromAeropyrum pernixK1 and examined their characteristics to clarify the active site of this enzyme. The enzyme was found to be a zinc-dependent metalloenzyme, containing one zinc ion for every monomer protein that was essential for activity. Site-directed mutagenesis of D144 increased the activity of the enzyme. Mutants D144N and D144A exhibited low affinity for the substrates and higher activity than the wild type, but their affinity for the zinc ion was the same as that of the wild type. Mutants D191N, H271A and H287A had a low affinity for the zinc ion and a low activity compared with the wild type. The double mutation, D191N/ H271A, had no enzyme activity and bound no zinc. From these results, it was clarified that residues D191, H271 and H287 participate in the catalytic activity of the enzyme by binding the zinc ion, and that D144 has an effect on substrate binding. The structure of the active site of Gro1PDH fromA. pernixK1 seems to be similar to that of glycerol dehydrogenase, despite the differences in substrate specificity and biological role.

  酶sn-甘油-1-磷酸脱氢酶（Gro1PDH，EC 1.1.1.261）对于古菌醚类脂质的甘油磷酸骨架（sn-甘油-1-磷酸）的对映构型形成至关重要。该酶催化二羟基乙酮磷酸和甘油-1-磷酸之间的可逆转化。迄今为止，尚未报道该酶的活性位点和催化机制信息。利用甘油脱氢酶的序列和结构信息，我们构建了Gro1PDH的六个突变体（D144N，D144A，D191N，H271A，H287A和D191N/H271A）来自Aeropyrum pernix K1，并检查了它们的特性以澄清该酶的活性位点。发现该酶是一种锌依赖性金属酶，每个单体蛋白质含有一个锌离子，对于活性至关重要。D144的位点定向突变增加了酶的活性。突变体D144N和D144A表现出对底物的亲和力较低，而活性比野生型高，但它们对锌离子的亲和力与野生型相同。突变体D191N，H271A和H287A与野生型相比，锌离子的亲和力和活性均较低。双重突变D191N/H271A没有酶活性，也没有结合锌离子。从这些结果可以澄清，残基D191、H271和H287通过结合锌离子参与了该酶的催化活性，而D144对底物结合有影响。尽管底物特异性和生物学作用有所不同，但Gro1PDH来自A. pernix K1的活性位点结构似乎类似于甘油脱氢酶。
• Reconstruction of the archaeal isoprenoid ether lipid biosynthesis pathway in Escherichia coli through digeranylgeranylglyceryl phosphate
  作者：Denton Lai、Ben Lluncor、Imke Schröder、Robert P. Gunsalus、James C. Liao、Harold G. Monbouquette

  DOI：10.1016/j.ymben.2009.01.008

  日期：2009.5

  unique isoprenoid biochemistry, which typically is based on two core lipid structures, sn-2,3-diphytanylglycerol diether (archaeol) and sn-2,3-dibiphytanyldiglycerol tetraether (caldarchaeol). The biosynthetic pathway for the tetraether lipid entails unprecedented head-to-head coupling of isoprenoid intermediates by an unknown mechanism involving unidentified enzymes. To investigate the isoprenoid ether

  古细菌的膜脂以独特的类异戊二烯生物化学为特征，其通常基于两个核心脂质结构，sn -2,3-二植烷酰基甘油二醚（古菌醇）和sn -2,3-二联植烷基二甘油四醚（caldarchaeol）。四醚脂质的生物合成途径需要类异戊二烯中间体通过未知机制进行前所未有的头对头偶联，其中包括未鉴定的酶。为了研究超嗜热古细菌Archaeoglobus fulgidus的类异戊二烯醚脂质生物合成途径，在工程大肠杆菌中重建了其脂质合成机制该菌株旨在首次证明有效的类异戊二烯醚脂质生物合成可用于生产中间体，二香叶基香叶基甘油基磷酸酯 (DGGGP)。使用LC / MS / MS技术DGGGP的生物合成进行了验证，并通过克隆和表达天然完成大肠杆菌基因为异戊烯基二磷酸（IPP）异构酶（IDI），与沿闪烁古生球菌基因G1P脱氢酶（EGSA ) 和 GGPP 合酶 ( gps )，在lac启动子的控制下。的闪烁古生球菌基因G
• Discovery and Functional Characterization of a Yeast Sugar Alcohol Phosphatase
  作者：Yi-Fan Xu、Wenyun Lu、Jonathan C. Chen、Sarah A. Johnson、Patrick A. Gibney、David G. Thomas、Greg Brown、Amanda L. May、Shawn R. Campagna、Alexander F. Yakunin、David Botstein、Joshua D. Rabinowitz

  DOI：10.1021/acschembio.8b00804

  日期：2018.10.19

  a sugar alcohol phosphatase. We term this enzyme, which hydrolyzes sorbitol-6-phosphate, ribitol-5-phosphate, and (d)-glycerol-3-phosphate, polyol phosphatase 1 or PYP1. Polyol phosphates are structural analogs of the enediol intermediate of phosphoglucose isomerase (Pgi). We find that sorbitol-6-phosphate and ribitol-5-phosphate inhibit Pgi and that Pyp1 activity is important for yeast to maintain

  糖醇（多元醇）在自然界广泛存在。尽管某些特定的糖醇磷酸酶是已知的，但对于某些重要的糖醇（例如，山梨糖醇6-磷酸酯）尚无已知的磷酸酶。使用基于液相色谱-质谱的代谢组学，我们筛选了具有未知功能的假定磷酸酶缺失的酵母菌株。我们显示酵母基因YNL010W，在所有真菌物种和某些植物中都有紧密的同源性，编码糖醇磷酸酶。我们术语此酶，它水解山梨糖醇-6-磷酸，核糖醇-5-磷酸，和（d） -甘油-3-磷酸，p醇ÿ醇p hosphatase 1或PYP1。多元醇磷酸酯是磷酸葡萄糖异构酶（Pgi）的烯二醇中间体的结构类似物。我们发现，山梨糖醇6-磷酸和核糖醇5-磷酸抑制Pgi，并且Pyp1活性对于在环境糖醇存在下维持Pgi活性的酵母很重要。Pyp1的表达与酵母的生长速度呈正相关，大概是因为更快的生长需要更大的糖酵解和相应的Pgi通量。因此，酵母表达以前未表征的酶Pyp1，以防止糖醇磷酸盐抑制糖酵解。Pyp1可能对工程糖醇生产有用。