PS 34:1 (BioDeep_00000632607)
Secondary id: BioDeep_00000009639
LipidSearch
代谢物信息卡片
化学式: C40H76NO10P (761.5207)
中文名称:
谱图信息:
最多检出来源 Homo sapiens(lipidomics) 94.28%
分子结构信息
SMILES: C(O)(=O)[C@@]([H])(N)COP(OC[C@]([H])(OC(CCCCCCC/C=C\CCCC)=O)COC(CCCCCCCCCCCCCCCCCCC)=O)(=O)O
InChI: InChI=1S/C40H76NO10P/c1-3-5-7-9-11-13-14-15-16-17-18-19-20-21-22-24-25-27-29-31-38(42)48-33-36(34-49-52(46,47)50-35-37(41)40(44)45)51-39(43)32-30-28-26-23-12-10-8-6-4-2/h17-18,36-37H,3-16,19-35,41H2,1-2H3,(H,44,45)(H,46,47)/b18-17-/t36-,37+/m1/s1
描述信息
A 3-sn-phosphatidyl-L-serine compound with a palmitoyl group at the 1-position and an oleoyl group at the 2-position.
同义名列表
49 个代谢物同义名
L-Serine, 3-[(1-oxohexadecyl)oxy]-2-[(1-oxo-9-octadecenyl)oxy]propyl hydrogen phosphate (ester), [R-(Z)]-; {1-O-hexadecanoyl-2-O-[(Z)-octadec-9-enoyl]-sn-glycero-3-phospho}serine; 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoserine; 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylserine; PS(16:0/18:1(9Z)); PS(16:0_18:1); PS(16:0/18:1); PS(34:1); PS 34:1; POPS; 1-(9Z-octadecenoyl)-2-hexadecanoyl-glycero-3-phosphoserine; PS(18:1(9Z)/16:0); 1-octadecanoyl-2-(9Z-hexadecenoyl)-glycero-3-phosphoserine; PS(18:0/16:1(9Z)); PS(16:1_18:0); 1-(11Z-docosenoyl)-2-dodecanoyl-glycero-3-phosphoserine; PS(22:1(11Z)/12:0); PS(12:0_22:1); 1-(11Z-eicosenoyl)-2-tetradecanoyl-glycero-3-phosphoserine; PS(20:1(11Z)/14:0); PS(14:0_20:1); 1-eicosanoyl-2-(9Z-tetradecenoyl)-glycero-3-phosphoserine; PS(20:0/14:1(9Z)); PS(14:1_20:0); 1-(9Z-nonadecenoyl)-2-pentadecanoyl-glycero-3-phosphoserine; PS(19:1(9Z)/15:0); PS(15:0_19:1); 1-nonadecanoyl-2-(9Z-pentadecenoyl)-glycero-3-phosphoserine; PS(19:0/15:1(9Z)); PS(15:1_19:0); 1-(9Z-heptadecenoyl)-2-heptadecanoyl-glycero-3-phosphoserine; PS(17:1(9Z)/17:0); PS(17:0_17:1); 1-heptadecanoyl-2-(9Z-heptadecenoyl)-glycero-3-phosphoserine; PS(17:0/17:1(9Z)); 1-(9Z-hexadecenoyl)-2-octadecanoyl-glycero-3-phosphoserine; PS(16:1(9Z)/18:0); 1-(9Z-pentadecenoyl)-2-nonadecanoyl-glycero-3-phosphoserine; PS(15:1(9Z)/19:0); 1-pentadecanoyl-2-(9Z-nonadecenoyl)-glycero-3-phosphoserine; PS(15:0/19:1(9Z)); 1-(9Z-tetradecenoyl)-2-eicosanoyl-glycero-3-phosphoserine; PS(14:1(9Z)/20:0); 1-tetradecanoyl-2-(11Z-eicosenoyl)-glycero-3-phosphoserine; PS(14:0/20:1(11Z)); 1-dodecanoyl-2-(11Z-docosenoyl)-glycero-3-phosphoserine; PS(12:0/22:1(11Z)); 1-hexadecanoyl-2-(11Z-octadecenoyl)-sn-glycero-3-phosphoserine; PS(16:0/18:1(11Z))
数据库引用编号
51 个数据库交叉引用编号
- ChEBI: CHEBI:181424
- ChEBI: CHEBI:34086
- ChEBI: CHEBI:75106
- ChEBI: CHEBI:90036
- ChEBI: CHEBI:170255
- ChEBI: CHEBI:170257
- ChEBI: CHEBI:90033
- ChEBI: CHEBI:170259
- ChEBI: CHEBI:170249
- ChEBI: CHEBI:170253
- KEGG: C13880
- PubChem: 5283499
- PubChem: 52926066
- PubChem: 52925996
- PubChem: 52925835
- PubChem: 52925640
- PubChem: 52925621
- PubChem: 52925594
- PubChem: 52925567
- PubChem: 52925366
- PubChem: 52925341
- PubChem: 52925321
- PubChem: 52925288
- PubChem: 52925259
- PubChem: 52925237
- PubChem: 52925212
- PubChem: 52925175
- PubChem: 9547073
- LipidMAPS: LMGP03010024
- LipidMAPS: LMGP03010959
- LipidMAPS: LMGP03010887
- LipidMAPS: LMGP03010725
- LipidMAPS: LMGP03010530
- LipidMAPS: LMGP03010511
- LipidMAPS: LMGP03010484
- LipidMAPS: LMGP03010457
- LipidMAPS: LMGP03010256
- LipidMAPS: LMGP03010231
- LipidMAPS: LMGP03010211
- LipidMAPS: LMGP03010178
- LipidMAPS: LMGP03010149
- LipidMAPS: LMGP03010127
- LipidMAPS: LMGP03010102
- LipidMAPS: LMGP03010065
- LipidMAPS: LMGP03010007
- CAS: 40290-44-6
- MetaboLights: MTBLC34086
- PubChem: 854125
- 3DMET: B05666
- NIKKAJI: J778.707C
- RefMet: PS 34:1
分类词条
相关代谢途径
Reactome(0)
BioCyc(0)
PlantCyc(0)
代谢反应
6 个相关的代谢反应过程信息。
Reactome(0)
BioCyc(0)
WikiPathways(0)
Plant Reactome(0)
INOH(0)
PlantCyc(0)
COVID-19 Disease Map(0)
PathBank(6)
- Phosphatidylethanolamine Biosynthesis PE(18:0/16:1(9Z)):
L-Serine + PC(18:0/16:1(9Z)) ⟶ Choline + PS(18:0/16:1(9Z))
- Phosphatidylethanolamine Biosynthesis PE(16:1(9Z)/18:0):
L-Serine + PC(16:1(9Z)/18:0) ⟶ Choline + PS(16:1(9Z)/18:0)
- Phosphatidylethanolamine Biosynthesis PE(16:1(9Z)/18:0):
L-Serine + PC(16:1(9Z)/18:0) ⟶ Choline + PS(16:1(9Z)/18:0)
- Phosphatidylethanolamine Biosynthesis PE(16:1(9Z)/18:0):
L-Serine + PC(16:1(9Z)/18:0) ⟶ Choline + PS(16:1(9Z)/18:0)
- Phosphatidylethanolamine Biosynthesis PE(16:1(9Z)/18:0):
L-Serine + PC(16:1(9Z)/18:0) ⟶ Choline + PS(16:1(9Z)/18:0)
- Array:
L-Serine + PC(16:1(9Z)/18:0) ⟶ Choline + PS(16:1(9Z)/18:0)
PharmGKB(0)
0 个相关的物种来源信息
在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:
- PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
- NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
- Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
- Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。
点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。
文献列表
- Ruitao Jin, Sitong He, Katrina A Black, Oliver B Clarke, Di Wu, Jani R Bolla, Paul Johnson, Agalya Periasamy, Ahmad Wardak, Peter Czabotar, Peter M Colman, Carol V Robinson, Derek Laver, Brian J Smith, Jacqueline M Gulbis. Ion currents through Kir potassium channels are gated by anionic lipids.
Nature communications.
2022 01; 13(1):490. doi:
10.1038/s41467-022-28148-4
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Journal of the American Chemical Society.
2021 11; 143(45):18899-18906. doi:
10.1021/jacs.1c05344
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Environment international.
2021 10; 155(?):106589. doi:
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The Journal of biological chemistry.
2021 Jan; 296(?):100159. doi:
10.1074/jbc.ra120.014618
. [PMID: 33277360] - Samantha Schrecke, Yun Zhu, Jacob W McCabe, Mariah Bartz, Charles Packianathan, Minglei Zhao, Ming Zhou, David Russell, Arthur Laganowsky. Selective regulation of human TRAAK channels by biologically active phospholipids.
Nature chemical biology.
2021 01; 17(1):89-95. doi:
10.1038/s41589-020-00659-5
. [PMID: 32989299] - P Gehan, S Kulifaj, P Soule, J B Bodin, M Amoura, A Walrant, S Sagan, A R Thiam, K Ngo, V Vivier, S Cribier, N Rodriguez. Penetratin translocation mechanism through asymmetric droplet interface bilayers.
Biochimica et biophysica acta. Biomembranes.
2020 11; 1862(11):183415. doi:
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. [PMID: 32710854] - Paulo Roberto Dores-Silva, David M Cauvi, Amanda L S Coto, Vanessa T R Kiraly, Júlio C Borges, Antonio De Maio. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain.
Cell stress & chaperones.
2020 11; 25(6):979-991. doi:
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. [PMID: 32725381] - Xubo Lin, Alemayehu A Gorfe. Transmembrane potential of physiologically relevant model membranes: Effects of membrane asymmetry.
The Journal of chemical physics.
2020 Sep; 153(10):105103. doi:
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. [PMID: 32933265] - Lisanna Sinisalu, Partho Sen, Samira Salihović, Suvi M Virtanen, Heikki Hyöty, Jorma Ilonen, Jorma Toppari, Riitta Veijola, Matej Orešič, Mikael Knip, Tuulia Hyötyläinen. Early-life exposure to perfluorinated alkyl substances modulates lipid metabolism in progression to celiac disease.
Environmental research.
2020 09; 188(?):109864. doi:
10.1016/j.envres.2020.109864
. [PMID: 32846648] - Larissa Smulders, Amanda J Daniels, Caroline B Plescia, Devon Berger, Robert V Stahelin, Nikolas Nikolaidis. Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A.
International journal of molecular sciences.
2020 Aug; 21(17):. doi:
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. [PMID: 32825419] - Maninder Singh, Vikash Kumar, Kamakshi Sikka, Ravi Thakur, Munesh Kumar Harioudh, Durga Prasad Mishra, Jimut Kanti Ghosh, Mohammad Imran Siddiqi. Computational Design of Biologically Active Anticancer Peptides and Their Interactions with Heterogeneous POPC/POPS Lipid Membranes.
Journal of chemical information and modeling.
2020 01; 60(1):332-341. doi:
10.1021/acs.jcim.9b00348
. [PMID: 31880450] - Josef Melcr, Tiago M Ferreira, Pavel Jungwirth, O H Samuli Ollila. Improved Cation Binding to Lipid Bilayers with Negatively Charged POPS by Effective Inclusion of Electronic Polarization.
Journal of chemical theory and computation.
2020 Jan; 16(1):738-748. doi:
10.1021/acs.jctc.9b00824
. [PMID: 31762275] - Alessandra Luchini, Frederik Grønbæk Tidemand, Nicolai Tidemand Johansen, Mario Campana, Javier Sotres, Michael Ploug, Marité Cárdenas, Lise Arleth. Peptide Disc Mediated Control of Membrane Protein Orientation in Supported Lipid Bilayers for Surface-Sensitive Investigations.
Analytical chemistry.
2020 01; 92(1):1081-1088. doi:
10.1021/acs.analchem.9b04125
. [PMID: 31769649] - Li-Ping Gao, Hai-Chao Chen, Ze-Lin Ma, An-Di Chen, Hong-Li Du, Jie Yin, Yu-Hong Jing. Fibrillation of human islet amyloid polypeptide and its toxicity to pancreatic β-cells under lipid environment.
Biochimica et biophysica acta. General subjects.
2020 01; 1864(1):129422. doi:
10.1016/j.bbagen.2019.129422
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Cell reports.
2019 12; 29(13):4583-4592.e3. doi:
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Scientific reports.
2019 12; 9(1):18349. doi:
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Molecules (Basel, Switzerland).
2019 Oct; 24(20):. doi:
10.3390/molecules24203739
. [PMID: 31627265] - Zhengjian Lv, Mohtadin Hashemi, Siddhartha Banerjee, Karen Zagorski, Jean-Christophe Rochet, Yuri L Lyubchenko. Assembly of α-synuclein aggregates on phospholipid bilayers.
Biochimica et biophysica acta. Proteins and proteomics.
2019 09; 1867(9):802-812. doi:
10.1016/j.bbapap.2019.06.006
. [PMID: 31226488] - Liang Xu, Shayon Bhattacharya, Damien Thompson. On the ubiquity of helical α-synuclein tetramers.
Physical chemistry chemical physics : PCCP.
2019 Jun; 21(22):12036-12043. doi:
10.1039/c9cp02464f
. [PMID: 31135803] - Caterina Ricci, Marco Maccarini, Peter Falus, Fabio Librizzi, Maria Rosalia Mangione, Oscar Moran, Maria Grazia Ortore, Ralf Schweins, Silvia Vilasi, Rita Carrotta. Amyloid β-Peptide Interaction with Membranes: Can Chaperones Change the Fate?.
The journal of physical chemistry. B.
2019 01; 123(3):631-638. doi:
10.1021/acs.jpcb.8b11719
. [PMID: 30569709] - José Carlos Bozelli, William Jennings, Stephanie Black, Yu Heng Hou, Darius Lameire, Preet Chatha, Tomohiro Kimura, Bob Berno, Adree Khondker, Maikel C Rheinstädter, Richard M Epand. Membrane curvature allosterically regulates the phosphatidylinositol cycle, controlling its rate and acyl-chain composition of its lipid intermediates.
The Journal of biological chemistry.
2018 11; 293(46):17780-17791. doi:
10.1074/jbc.ra118.005293
. [PMID: 30237168] - Chris Neale, Angel E García. Methionine 170 is an Environmentally Sensitive Membrane Anchor in the Disordered HVR of K-Ras4B.
The journal of physical chemistry. B.
2018 11; 122(44):10086-10096. doi:
10.1021/acs.jpcb.8b07919
. [PMID: 30351122] - Mason L Valentine, Alfredo E Cardenas, Ron Elber, Carlos R Baiz. Physiological Calcium Concentrations Slow Dynamics at the Lipid-Water Interface.
Biophysical journal.
2018 10; 115(8):1541-1551. doi:
10.1016/j.bpj.2018.08.044
. [PMID: 30269885] - Xubo Lin, Hongyin Wang, Zhichao Lou, Meng Cao, Zuoheng Zhang, Ning Gu. Roles of PIP2 in the membrane binding of MIM I-BAR: insights from molecular dynamics simulations.
FEBS letters.
2018 08; 592(15):2533-2542. doi:
10.1002/1873-3468.13186
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Biochimica et biophysica acta. Molecular and cell biology of lipids.
2018 Apr; 1863(4):349-358. doi:
10.1016/j.bbalip.2018.01.001
. [PMID: 29306076] - Tatsuro Goda, Yuji Miyahara. Specific binding of human C-reactive protein towards supported monolayers of binary and engineered phospholipids.
Colloids and surfaces. B, Biointerfaces.
2018 Jan; 161(?):662-669. doi:
10.1016/j.colsurfb.2017.11.036
. [PMID: 29172154] - Milka Doktorova, Frederick A Heberle, Richard L Kingston, George Khelashvili, Michel A Cuendet, Yi Wen, John Katsaras, Gerald W Feigenson, Volker M Vogt, Robert A Dick. Cholesterol Promotes Protein Binding by Affecting Membrane Electrostatics and Solvation Properties.
Biophysical journal.
2017 Nov; 113(9):2004-2015. doi:
10.1016/j.bpj.2017.08.055
. [PMID: 29117524] - Helen Y Fan, Heiko Heerklotz. Digitonin does not flip across cholesterol-poor membranes.
Journal of colloid and interface science.
2017 Oct; 504(?):283-293. doi:
10.1016/j.jcis.2017.05.034
. [PMID: 28551523] - Jeevan B Gc, Bernard S Gerstman, Prem P Chapagain. Membrane association and localization dynamics of the Ebola virus matrix protein VP40.
Biochimica et biophysica acta. Biomembranes.
2017 Oct; 1859(10):2012-2020. doi:
10.1016/j.bbamem.2017.07.007
. [PMID: 28711356] - Ellen M Muehl, Joshua M Gajsiewicz, Sara M Medfisch, Zachary S B Wiersma, James H Morrissey, Ryan C Bailey. Multiplexed silicon photonic sensor arrays enable facile characterization of coagulation protein binding to nanodiscs with variable lipid content.
The Journal of biological chemistry.
2017 09; 292(39):16249-16256. doi:
10.1074/jbc.m117.800938
. [PMID: 28801460] - Justine Wolf, Christopher Aisenbrey, Nicole Harmouche, Jesus Raya, Philippe Bertani, Natalia Voievoda, Regine Süss, Burkhard Bechinger. pH-Dependent Membrane Interactions of the Histidine-Rich Cell-Penetrating Peptide LAH4-L1.
Biophysical journal.
2017 Sep; 113(6):1290-1300. doi:
10.1016/j.bpj.2017.06.053
. [PMID: 28734478] - Rafal Zdanowicz, Alex Kreutzberger, Binyong Liang, Volker Kiessling, Lukas K Tamm, David S Cafiso. Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.
Biophysical journal.
2017 Sep; 113(6):1235-1250. doi:
10.1016/j.bpj.2017.04.002
. [PMID: 28456331] - Antreas C Kalli, Tomasz Rog, Ilpo Vattulainen, Iain D Campbell, Mark S P Sansom. The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.
The Journal of membrane biology.
2017 08; 250(4):337-351. doi:
10.1007/s00232-016-9908-z
. [PMID: 27465729] - Eileen Edler, Eric Schulze, Matthias Stein. Membrane localization and dynamics of geranylgeranylated Rab5 hypervariable region.
Biochimica et biophysica acta. Biomembranes.
2017 Aug; 1859(8):1335-1349. doi:
10.1016/j.bbamem.2017.04.021
. [PMID: 28455099] - Shruti Mukherjee, Rajiv K Kar, Ravi Prakash Reddy Nanga, Kamal H Mroue, Ayyalusamy Ramamoorthy, Anirban Bhunia. Accelerated molecular dynamics simulation analysis of MSI-594 in a lipid bilayer.
Physical chemistry chemical physics : PCCP.
2017 Jul; 19(29):19289-19299. doi:
10.1039/c7cp01941f
. [PMID: 28702543] - Elaheh Jamasbi, Frances Separovic, Mohammed Akhter Hossain, Giuseppe Donato Ciccotosto. Phosphorylation of a full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties.
Molecular bioSystems.
2017 Jul; 13(8):1545-1551. doi:
10.1039/c7mb00249a
. [PMID: 28642958] - Maria A Soria, Silvia A Cervantes, Thalia H Bajakian, Ansgar B Siemer. The Functional Amyloid Orb2A Binds to Lipid Membranes.
Biophysical journal.
2017 Jul; 113(1):37-47. doi:
10.1016/j.bpj.2017.05.039
. [PMID: 28700922] - Dayane S Alvares, João Ruggiero Neto, Ernesto E Ambroggio. Phosphatidylserine lipids and membrane order precisely regulate the activity of Polybia-MP1 peptide.
Biochimica et biophysica acta. Biomembranes.
2017 Jun; 1859(6):1067-1074. doi:
10.1016/j.bbamem.2017.03.002
. [PMID: 28274844] - Kaveesha J Wijesinghe, Sarah Urata, Nisha Bhattarai, Edgar E Kooijman, Bernard S Gerstman, Prem P Chapagain, Sheng Li, Robert V Stahelin. Detection of lipid-induced structural changes of the Marburg virus matrix protein VP40 using hydrogen/deuterium exchange-mass spectrometry.
The Journal of biological chemistry.
2017 04; 292(15):6108-6122. doi:
10.1074/jbc.m116.758300
. [PMID: 28167534] - Tao Ni, Antreas C Kalli, Fiona B Naughton, Luke A Yates, Omar Naneh, Mirijam Kozorog, Gregor Anderluh, Mark S P Sansom, Robert J C Gilbert. Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain.
The Biochemical journal.
2017 02; 474(4):539-556. doi:
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. [PMID: 27974389] - Patrick Drücker, Andreas Rühling, David Grill, Da Wang, Annette Draeger, Volker Gerke, Frank Glorius, Hans-Joachim Galla. Imidazolium Salts Mimicking the Structure of Natural Lipids Exploit Remarkable Properties Forming Lamellar Phases and Giant Vesicles.
Langmuir : the ACS journal of surfaces and colloids.
2017 02; 33(6):1333-1342. doi:
10.1021/acs.langmuir.6b03182
. [PMID: 27935708] - Xiaoxue Zhang, Johnna R St Clair, Erwin London, Daniel P Raleigh. Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.
Biochemistry.
2017 Jan; 56(2):376-390. doi:
10.1021/acs.biochem.6b01016
. [PMID: 28054763] - Davit Hakobyan, Volker Gerke, Andreas Heuer. Modeling of annexin A2-Membrane interactions by molecular dynamics simulations.
PloS one.
2017; 12(9):e0185440. doi:
10.1371/journal.pone.0185440
. [PMID: 28937994] - Kari Kusler, Samuel O Odoh, Alexey Silakov, Matthew F Poyton, Saranya Pullanchery, Paul S Cremer, Laura Gagliardi. What Is the Preferred Conformation of Phosphatidylserine-Copper(II) Complexes? A Combined Theoretical and Experimental Investigation.
The journal of physical chemistry. B.
2016 12; 120(50):12883-12889. doi:
10.1021/acs.jpcb.6b10675
. [PMID: 27957849] - Himanshu Chaudhary, Aditya Iyer, Vinod Subramaniam, Mireille M A E Claessens. α-Synuclein Oligomers Stabilize Pre-Existing Defects in Supported Bilayers and Propagate Membrane Damage in a Fractal-Like Pattern.
Langmuir : the ACS journal of surfaces and colloids.
2016 11; 32(45):11827-11836. doi:
10.1021/acs.langmuir.6b02572
. [PMID: 27766878] - Jan K Marzinek, Daniel A Holdbrook, Roland G Huber, Chandra Verma, Peter J Bond. Pushing the Envelope: Dengue Viral Membrane Coaxed into Shape by Molecular Simulations.
Structure (London, England : 1993).
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