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Human Metabolome Database Version 2.5

 

Showing metabocard for Stearidonic acid (HMDB06547)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-23 16:30:04
Update Date 2010-07-22 11:30:37
Accession Number HMDB06547
Secondary Accession Numbers Not Available
Common Name Stearidonic acid
Description Stearidonic acid is found in dietary plant oils which are metabolized to longer-chain, more unsaturated (n-3) PUFA. These oils appear to possess hypotriglyceridemic properties typically associated with fish oils.(PMID: 15173404) stearidonic acid may be used as a precursor to increase the EPA content of human lipids and that combinations of gamma-linolenic acid and stearidonic acid eicosapentaenoic acid can be used to manipulate the fatty acid compositions of lipid pools in subtle ways. Such effects may offer new strategies for manipulation of cell composition in order to influence cellular responses and functions in desirable ways. (PMID: 15120716)
Synonyms
  1. Stearidonic acid
  2. 6,9,12,15-octadecatetraenoic acid
  3. stearidonic acid C18:4
  4. 6,9,12,15-octadecatetraenoate
Chemical IUPAC Name (6Z,9Z,12Z,15Z)-octadeca-6,9,12,15-tetraenoic acid
Chemical Formula C18H28O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Fatty Acids
Sub Class
  • Long chain fatty acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • alkene
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 276.414
Monoisotopic Molecular Weight 276.208923
Isomeric SMILES CCC=C/CC=C/CC=C/CC=C/CCCCC(O)=O
Canonical SMILES CCC=CCC=CCC=CCC=CCCCCC(O)=O
KEGG Compound ID C16300 Link Image
BioCyc ID Not Available
BiGG ID 2218006 Link Image
Wikipedia Link Stearidonic acid Link Image
NuGOwiki Link HMDB06547 Link Image
Metagene Link HMDB06547 Link Image
METLIN ID Not Available
PubChem Compound 5282837 Link Image
PubChem Substance 7850034 Link Image
ChEBI ID 32389 Link Image
CAS Registry Number 20290-75-9
InChI Identifier InChI=1/C18H28O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18(19)20/h3-4,6-7,9-10,12-13H,2,5,8,11,14-17H2,1H3,(H,19,20)/b4-3-,7-6-,10-9-,13-12-
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.02e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5.5 [Predicted by PubChem via XLOGP]; 6.19 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.016 +/- 0.001 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Quehenberger O, Armando AM, Brown AH, Milne SB, Myers DS, Merrill AH, Bandyopadhyay S, Jones KN, Kelly S, Shaner RL, Sullards CM, Wang E, Murphy RC, Barkley RM, Leiker TJ, Raetz CR, Guan Z, Laird GM, Six DA, Russell DW, McDonald JG, Subramaniam S, Fahy E, Dennis EA: Lipidomics reveals a remarkable diversity of lipids in human plasma. J Lipid Res. 2010 Nov;51(11):3299-305. Epub 2010 Jul 29. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Alpha Linolenic Acid and Linoleic Acid Metabolism SMP00018 Link Image map00592 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Fatty acid desaturase 2
Enzyme 1 [top]
Enzyme 1 ID 8800
Enzyme 1 Name Fatty acid desaturase 2
Enzyme 1 Synonyms
  1. Delta(6) fatty acid desaturase
  2. D6D
  3. Delta(6) desaturase
Enzyme 1 Gene Name FADS2
Enzyme 1 Protein Sequence >Fatty acid desaturase 2
MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVI
GHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTA
EDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQH
DYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFV
LGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAV
SYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQL
TATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLL
RALLDIIRSLKKSGKLWLDAYLHK
Enzyme 1 Number of Residues 444
Enzyme 1 Molecular Weight 52259.1
Enzyme 1 Theoretical pI 9.18
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
  • transition metal ion binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid biosynthetic process
  • fatty acid metabolic process
  • lipid metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
  • primary metabolic process
Component
Enzyme 1 General Function Involved in heme binding
Enzyme 1 Specific Function Component of a lipid metabolic pathway that catalyzes biosynthesis of highly unsaturated fatty acids (HUFA) from precursor essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3). Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma- linoleic acid (GLA) (18:3n-6) and stearidonic acid (18:4n-3) respectively and other desaturation steps. Highly unsaturated fatty acids (HUFA) play pivotal roles in many biological functions. It catalizes as well the introduction of a cis double bond in palmitate to produce the mono-unsaturated fatty acid sapienate, the most abundant fatty acid in sebum
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 132-152 158-178 265-285 306-326
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID O95864 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FADS2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1335 bp
ATGGGGAAGGGAGGGAACCAGGGCGAGGGGGCCGCCGAGCGCGAGGTGTCGGTGCCCACC
TTCAGCTGGGAGGAGATTCAGAAGCATAACCTGCGCACCGACAGGTGGCTGGTCATTGAC
CGCAAGGTTTACAACATCACCAAATGGTCCATCCAGCACCCGGGGGGCCAGCGGGTCATC
GGGCACTACGCTGGAGAAGATGCAACGGATGCCTTCCGCGCCTTCCACCCTGACCTGGAA
TTCGTGGGCAAGTTCTTGAAACCCCTGCTGATTGGTGAACTGGCCCCGGAGGAGCCCAGC
CAGGACCACGGCAAGAACTCAAAGATCACTGAGGACTTCCGGGCCCTGAGGAAGACGGCT
GAGGACATGAACCTGTTCAAGACCAACCACGTGTTCTTCCTCCTCCTCCTGGCCCACATC
ATCGCCCTGGAGAGCATTGCATGGTTCACTGTCTTTTACTTTGGCAATGGCTGGATTCCT
ACCCTCATCACGGCCTTTGTCCTTGCTACCTCTCAGGCCCAAGCTGGATGGCTGCAACAT
GATTATGGCCACCTGTCTGTCTACAGAAAACCCAAGTGGAACCACCTTGTCCACAAATTC
GTCATTGGCCACTTAAAGGGTGCCTCTGCCAACTGGTGGAATCATCGCCACTTCCAGCAC
CACGCCAAGCCTAACATCTTCCACAAGGATCCCGATGTGAACATGCTGCACGTGTTTGTT
CTGGGCGAATGGCAGCCCATCGAGTACGGCAAGAAGAAGCTGAAATACCTGCCCTACAAT
CACCAGCACGAATACTTCTTCCTGATTGGGCCGCCGCTGCTCATCCCCATGTATTTCCAG
TACCAGATTATCATGACCATGATCGTCCATAAGAACTGGGTGGACCTGGCCTGGGCCGTC
AGCTACTACATCCGGTTCTTCATCACCTACATCCCTTTCTACGGCATCCTGGGAGCCCTC
CTTTTCCTCAACTTCATCAGGTTCCTGGAGAGCCACTGGTTTGTGTGGGTCACACAGATG
AATCACATCGTCATGGAGATTGACCAGGAGGCCTACCGTGACTGGTTCAGTAGCCAGCTG
ACAGCCACCTGCAACGTGGAGCAGTCCTTCTTCAACGACTGGTTCAGTGGACACCTTAAC
TTCCAGATTGAGCACCACCTCTTCCCCACCATGCCCCGGCACAACTTACACAAGATCGCC
CCGCTGGTGAAGTCTCTATGTGCCAAGCATGGCATTGAATACCAGGAGAAGCCGCTACTG
AGGGCCCTGCTGGACATCATCAGGTCCCTGAAGAAGTCTGGGAAGCTGTGGCTGGACGCC
TACCTTCACAAATGA
Enzyme 1 GenBank Gene ID AF126799 Link Image
Enzyme 1 GeneCard ID FADS2 Link Image
Enzyme 1 GenAtlas ID FADS2 Link Image
Enzyme 1 HGNC ID HGNC:3575 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 11q12.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Cho HP, Nakamura MT, Clarke SD: Cloning, expression, and nutritional regulation of the mammalian Delta-6 desaturase. J Biol Chem. 1999 Jan 1;274(1):471-7. [PubMed Link Image]
  2. Marquardt A, Stohr H, White K, Weber BH: cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family. Genomics. 2000 Jun 1;66(2):175-83. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  7. Nara TY, He WS, Tang C, Clarke SD, Nakamura MT: The E-box like sterol regulatory element mediates the suppression of human Delta-6 desaturase gene by highly unsaturated fatty acids. Biochem Biophys Res Commun. 2002 Aug 9;296(1):111-7. [PubMed Link Image]
  8. Ge L, Gordon JS, Hsuan C, Stenn K, Prouty SM: Identification of the delta-6 desaturase of human sebaceous glands: expression and enzyme activity. J Invest Dermatol. 2003 May;120(5):707-14. [PubMed Link Image]
  9. Tang C, Cho HP, Nakamura MT, Clarke SD: Regulation of human delta-6 desaturase gene transcription: identification of a functional direct repeat-1 element. J Lipid Res. 2003 Apr;44(4):686-95. Epub 2003 Jan 16. [PubMed Link Image]
  10. Lane J, Mansel RE, Jiang WG: Expression of human delta-6-desaturase is associated with aggressiveness of human breast cancer. Int J Mol Med. 2003 Aug;12(2):253-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available