Dihydroxyacetone phosphate
(Synonyms: 1-HYDROXY-3-(PHOSPHONOOXY)-2-PROPANONE半镁盐) 目录号 : GC35865
A glycerolipid precursor
Cas No.:57-04-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Dihydroxyacetone phosphate is a precursor in the biosynthesis of glycerolipids.1 It is produced by the glycolytic enzyme fructose-1,6-bisphosphate aldolase or by isomerization of glyceraldehyde-3-phosphate by triosephosphate isomerase.2 Erythrocyte levels of dihydroxyacetone phosphate are increased in patients with triosephosphate isomerase deficiency, an inborn error of metabolism characterized by hemolytic anemia and progressive neurological dysfunction.3
1.Dodds, P.F., Gurr, M.I., and Brindley, D.N.The glycerol phosphate, dihydroxyacetone phosphate and monoacylglycerol pathways of glycerolipid synthesis in rat adipose-tissue homogenatesBiochem J.160(3)693-700(1976) 2.Miyazawa, H., Yamaguchi, Y., Sugiura, Y., et al.Rewiring of embryonic glucose metabolism via suppression of PFK-1 and aldolase during mouse chorioallantoic branchingDevelopment144(1)63-73(2017) 3.Orosz, F., Vértessy, B.G., Hollán, S., et al.Triosephosphate isomerase deficiency: Predictions and factsJ. Theor. Biol.182(3)437-447(1996)
| Cas No. | 57-04-5 | SDF | |
| 别名 | 1-HYDROXY-3-(PHOSPHONOOXY)-2-PROPANONE半镁盐 | ||
| Canonical SMILES | O=C(COP(O)(O)=O)CO | ||
| 分子式 | C3H7O6P | 分子量 | 170.06 |
| 溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 5.8803 mL | 29.4014 mL | 58.8028 mL |
| 5 mM | 1.1761 mL | 5.8803 mL | 11.7606 mL |
| 10 mM | 0.588 mL | 2.9401 mL | 5.8803 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Dihydroxyacetone phosphate signals glucose availability to mTORC1
Nat Metab 2020 Sep;2(9):893-901.PMID:32719541DOI:10.1038/s42255-020-0250-5.
The mechanistic target of rapamycin complex 1 (mTORC1) kinase regulates cell growth by setting the balance between anabolic and catabolic processes. To be active, mTORC1 requires the environmental presence of amino acids and glucose. While a mechanistic understanding of amino acid sensing by mTORC1 is emerging, how glucose activates mTORC1 remains mysterious. Here, we used metabolically engineered human cells lacking the canonical energy sensor AMP-activated protein kinase to identify glucose-derived metabolites required to activate mTORC1 independent of energetic stress. We show that mTORC1 senses a metabolite downstream of the aldolase and upstream of the GAPDH-catalysed steps of glycolysis and pinpoint Dihydroxyacetone phosphate (DHAP) as the key molecule. In cells expressing a triose kinase, the synthesis of DHAP from DHA is sufficient to activate mTORC1 even in the absence of glucose. DHAP is a precursor for lipid synthesis, a process under the control of mTORC1, which provides a potential rationale for the sensing of DHAP by mTORC1.
Nuclear Dihydroxyacetone phosphate signals nutrient sufficiency and cell cycle phase to global histone acetylation
Nat Metab 2021 Jun;3(6):859-875.PMID:34140692DOI:10.1038/s42255-021-00405-8.
Global histone acetylation varies with changes in the nutrient and cell cycle phases; however, the mechanisms connecting these variations are not fully understood. Herein, we report that nutrient-related and cell-cycle-regulated nuclear acetate regulates global histone acetylation. Histone deacetylation-generated acetate accumulates in the nucleus and induces histone hyperacetylation. The nuclear acetate levels were controlled by glycolytic enzyme triosephosphate isomerase 1 (TPI1). Cyclin-dependent kinase 2 (CDK2), which is phosphorylated and activated by nutrient-activated mTORC1, phosphorylates TPI1 Ser 117 and promotes nuclear translocation of TPI1, decreases nuclear Dihydroxyacetone phosphate (DHAP) and induces nuclear acetate accumulation because DHAP scavenges acetate via the formation of 1-acetyl-DHAP. CDK2 accumulates in the cytosol during the late G1/S phases. Inactivation or blockade of nuclear translocation of TPI1 abrogates nutrient-dependent and cell-cycle-dependent global histone acetylation, chromatin condensation, gene transcription and DNA replication. These results identify the mechanism of maintaining global histone acetylation by nutrient and cell cycle signals.
Chemical and enzymatic routes to Dihydroxyacetone phosphate
Appl Microbiol Biotechnol 2007 May;75(1):33-45.PMID:17318530DOI:10.1007/s00253-007-0882-3.
Stereoselective carbon-carbon bond formation with aldolases has become an indispensable tool in preparative synthetic chemistry. In particular, the Dihydroxyacetone phosphate (DHAP)-dependent aldolases are attractive because four different types are available that allow access to a complete set of diastereomers of vicinal diols from achiral aldehyde acceptors and the DHAP donor substrate. While the substrate specificity for the acceptor is rather relaxed, these enzymes show only very limited tolerance for substituting the donor. Therefore, access to DHAP is instrumental for the preparative exploitation of these enzymes, and several routes for its synthesis have become available. DHAP is unstable, so chemical synthetic routes have concentrated on producing a storable precursor that can easily be converted to DHAP immediately before its use. Enzymatic routes have concentrated on integrating the DHAP formation with upstream or downstream catalytic steps, leading to multi-enzyme arrangements with up to seven enzymes operating simultaneously. While the various chemical routes suffer from either low yields, complicated work-up, or toxic reagents or catalysts, the enzymatic routes suffer from complex product mixtures and the need to assemble multiple enzymes into one reaction scheme. Both types of routes will require further improvement to serve as a basis for a scalable route to DHAP.
Alkyl Dihydroxyacetone phosphate synthase in glycosomes of Trypanosoma brucei
Biochim Biophys Acta 1995 Jul 13;1257(2):167-73.PMID:7619857DOI:10.1016/0005-2760(95)00066-l.
Alkyl-dihydroxyacetone phosphate synthase (E.C. 2.5.1.26), the key enzyme in ether phospholipid biosynthesis, was demonstrated to be present in Trypanosoma brucei. The distribution of alkyl-dihydroxyacetone phosphate synthase was found to be identical to that of Dihydroxyacetone phosphate acyltransferase (E.C. 2.3.1.42), which has previously been shown to be exclusively associated with the glycosome fraction (Opperdoes, F.R. (1984) FEBS Lett. 169, 35-39). Studies with gradient purified glycosomes indicated that the formation of alkyl-dihydroxyacetone phosphate was completely dependent on the presence of acyl-dihydroxyacetone phosphate. The glycosomal alkyl-dihydroxyacetone phosphate synthase activity was characterized with respect to its pH optimum, Triton X-100 sensitivity and the dependency on the concentration of the substrates palmitoyl-dihydroxyacetone phosphate and hexadecanol. Using thin-layer chromatographic and alkaline hydrolysis procedures the reaction product was identified as alkyl-dihydroxyacetone phosphate. Alkyl-dihydroxyacetone phosphate synthase was resistant to proteolytic inactivation by trypsin in intact glycosomes but not in Triton X-100 disrupted glycosomes. It is concluded that T. brucei glycosomes contain the enzymes responsible for glycero-ether bond formation analogous to mammalian peroxisomes.
Dihydroxyacetone phosphate reductase in plants
Plant Physiol 1988 Jan;86(1):98-103.PMID:16665901DOI:10.1104/pp.86.1.98.
Two forms of Dihydroxyacetone phosphate reductase are present in spinach, soybean, pea, and mesophyll cells of corn leaves. An improved homogenizing medium was developed to measure this activity. The enzyme was detectable only after dialysis of the 35 to 70% saturated (NH(4))(2)SO(4) fraction and the two forms were separated by chromatography on either DEAE cellulose or Sephacryl S-200. About 80% of the reductase was one form in the chloroplast and the rest was a second form in the cytosol as determined by chromatography and by fractionation of subcellular organelles. The amount of activity detectable in the chloroplast fraction was 10.7 micromoles of Dihydroxyacetone phosphate reductase per hour per milligram chlorophyll from spinach leaves and 4.9 from pea leaves. The chloroplast form eluted first from DEAE cellulose and, being smaller, it eluted second from Sephacryl S-200. Activity of the chloroplast form was stimulated 3- to 5-fold by the addition of 1 millimolar dithiothreitol or 50 microgram reduced Escherichia coli thioredoxin or 4 micrograms spinach thioredoxin to the assay mixture. This stimulation was not observed with monothiols. Activity of the cytosolic form was not affected by either reduced thioredoxin or dithiothreitol.