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Human Metabolome Database Version 2.5

 

Showing metabocard for Hexacosanoic acid (HMDB02356)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:49
Update Date 2009-11-24 21:51:36
Accession Number HMDB02356
Secondary Accession Numbers Not Available
Common Name Hexacosanoic acid
Description X-linked adrenoleukodystrophy (X-ALD) is a peroxisomal disorder biochemically characterized by the accumulation of very long chain fatty acids (VLCFA), particularly hexacosanoic acid (C(26:0)) and tetracosanoic acid (C(24:0)), in tissues and biological fluids. (PMID 16750542)
Synonyms
  1. Cerate
  2. Ceratinate
  3. Ceratinic acid
  4. Ceric acid
  5. Cerinate
  6. Cerinic acid
  7. Cerotic acid
  8. Cerylate
  9. Cerylic acid
  10. Hexacosanoate
  11. hexacosanoate (n-C26:0)
  12. n-Hexacosanoate
  13. n-Hexacosanoic acid
  14. Hexacosanoic acid
Chemical IUPAC Name hexacosanoic acid
Chemical Formula C26H52O2
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
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 396.690
Monoisotopic Molecular Weight 396.396729
Isomeric SMILES CCCCCCCCCCCCCCCCCCCCCCCCCC(O)=O
Canonical SMILES CCCCCCCCCCCCCCCCCCCCCCCCCC(O)=O
KEGG Compound ID Not Available
BioCyc ID 2-PG Link Image
BiGG ID 1459812 Link Image
Wikipedia Link Cerate Link Image
NuGOwiki Link HMDB02356 Link Image
Metagene Link HMDB02356 Link Image
METLIN ID 6642 Link Image
PubChem Compound 10469 Link Image
PubChem Substance 6863424 Link Image
ChEBI ID 31009 Link Image
CAS Registry Number 506-46-7
InChI Identifier InChI=1/C26H52O2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18-19-20-21-22-23-24-25-26(27)28/h2-25H2,1H3,(H,27,28)
Synthesis Reference Tsuji S; Sano T; Ariga T; Miyatake T Increased synthesis of hexacosanoic acid (C23:0) by cultured skin fibroblasts from patients with adrenoleukodystrophy (ALD) and adrenomyeloneuropathy (AMN). Journal of biochemistry (1981), 90(4), 1233-6.
Melting Point (Experimental) 88.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.81e-05 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 9.87 [Predicted by ALOGPS]; 10.7 [Predicted by PubChem via XLOGP]; 11.87 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
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High Energy
Download File
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Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
Tissue Location
Tissue References
Adrenal Gland —
Fibroblasts —
Concentrations (Normal)
Biofluid Blood
Value 0.83 +/- 0.45 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Sadeghi-Nejad A, Senior B: Adrenomyeloneuropathy presenting as Addison's disease in childhood. N Engl J Med. 1990 Jan 4;322(1):13-6. [PubMed Link Image]
Biofluid Blood
Value 0.88 (0.25-1.5) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 4.10 (2.42 - 6.43) uM
Age Adult:>18 yrs old
Sex Both
Condition Adrenomyeloneuropathy
Comments Not Available
References
  • Sadeghi-Nejad A, Senior B: Adrenomyeloneuropathy presenting as Addison's disease in childhood. N Engl J Med. 1990 Jan 4;322(1):13-6. [PubMed Link Image]
Biofluid Blood
Value 8.8 (2.5-15.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Adrenoleukodystrophy
Comments Not Available
References
Biofluid Blood
Value 2.0 (2.0-2.09) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Associated Disorders
Condition References
Adrenoleukodystrophy
Adrenomyeloneuropathy
  • Sadeghi-Nejad A, Senior B: Adrenomyeloneuropathy presenting as Addison's disease in childhood. N Engl J Med. 1990 Jan 4;322(1):13-6. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Beta Oxidation of Very Long Chain Fatty Acids SMP00052 Link Image map01040 Link Image
General References
  1. Moser HW, Moser AB, Powers JM, Nitowsky HM, Schaumburg HH, Norum RA, Migeon BR: The prenatal diagnosis of adrenoleukodystrophy. Demonstration of increased hexacosanoic acid levels in cultured amniocytes and fetal adrenal gland. Pediatr Res. 1982 Mar;16(3):172-5. [PubMed Link Image]
  2. Dhaunsi GS, Kaur J, Alsaeid K, Turner RB, Bitar MS: Very long chain fatty acids activate NADPH oxidase in human dermal fibroblasts. Cell Biochem Funct. 2005 Jan-Feb;23(1):65-8. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Long-chain-fatty-acid--CoA ligase 1
Enzyme 1 [top]
Enzyme 1 ID 5849
Enzyme 1 Name Long-chain-fatty-acid--CoA ligase 1
Enzyme 1 Synonyms
  1. Long-chain acyl-CoA synthetase 1
  2. LACS 1
  3. Palmitoyl-CoA ligase 1
  4. Long-chain fatty acid CoA ligase 2
  5. Long-chain acyl-CoA synthetase 2
  6. LACS 2
  7. Acyl-CoA synthetase 1
  8. ACS1
  9. Palmitoyl-CoA ligase 2
Enzyme 1 Gene Name ACSL1
Enzyme 1 Protein Sequence >Long-chain-fatty-acid--CoA ligase 1 
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQ
SVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEW
LSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT
LGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQR
CGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAF
VKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQP
TVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKV
QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV
GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGD
IGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAI
VVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHP
ELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
Enzyme 1 Number of Residues 698
Enzyme 1 Molecular Weight 77944
Enzyme 1 Theoretical pI 7.16
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 25-45
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 219900 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P33121 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACSL1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2097 bp 
ATGCAAGCCCATGAGCTGTTCCGGTATTTTCGAATGCCAGAGCTGGTTGACTTCCGACAG
TACGTGCGTACTCTTCCGACCAACACGCTTATGGGCTTCGGAGCTTTTGCAGCACTCACC
ACCTTCTGGTACGCCACGAGACCCAAACCCCTGAAGCCGCCATGCGACCTCTCCATGCAG
TCAGTGGAAGTGGCGGGTAGTGGTGGTGCACGAAGATCCGCACTACTTGACAGCGACGAG
CCCTTGGTGTATTTCTATGATGATGTCACAACATTATACGAAGGTTTCCAGAGGGGAATA
CAGGTGTCAAATAATGGCCCTTGTTTAGGCTCTCGGAAACCAGACCAACCCTATGAATGG
CTTTCATATAAACAGGTTGCAGAATTGTCGGAGTGCATAGGCTCAGCACTGATCCAGAAG
GGCTTCAAGACTGCCCCAGATCAGTTCATTGGCATCTTTGCTCAAAATAGACCTGAGTGG
GTGATTATTGAACAAGGATGCTTTGCTTATTCGATGGTGATCGTTCCACTTTATGATACC
CTTGGAAATGAAGCCATCACGTACATAGTCAACAAAGCTGAACTCTCTCTGGTTTTTGTT
GACAAGCCAGAGAAGGCCAAACTCTTATTAGAGGGTGTAGAAAATAAGTTAATACCAGGC
CTTAAAATCATAGTTGTCATGGATGCCTACGGCAGTGAACTGGTGGAACGAGGCCAGAGG
TGTGGGGTGGAAGTCACCAGCATGAAGGCGATGGAGGACCTGGGAAGAGCCAACAGACGG
AAGCCCAAGCCTCCAGCACCTGAAGATCTTGCAGTAATTTGTTTCACAAGTGGAACTACA
GGCAACCCCAAAGGAGCAATGGTCACTCACCGAAACATAGTGAGCGATTGTTCAGCTTTT
GTGAAAGCAACAGAGAATACAGTCAATCCTTGCCCAGATGATACTTTGATATCTTTCTTG
CCTCTCGCCCATATGTTTGAGAGAGTTGTAGAGTGTGTAATGCTGTGTCATGGAGCTAAA
ATCGGATTTTTCCAAGGAGATATCAGGCTGCTCATGGATGACCTCAAGGTGCTTCAACCC
ACTGTCTTCCCCGTGGTTCCAAGACTGCTGAACCGGATGTTTGACCGAATTTTCGGACAA
GCAAACACCACGCTGAAGCGATGGCTCTTGGACTTTGCCTCCAAGAGGAAAGAAGCAGAG
CTTCGCAGCGGCATCATCAGAAACAACAGCCTGTGGGACCGGCTGATCTTCCACAAAGTA
CAGTCGAGCCTGGGCGGAAGAGTCCGGCTGATGGTGACAGGAGCCGCCCCGGTGTCTGCC
ACTGTGCTGACGTTCCTCAGAGCAGCCCTGGGCTGTCAGTTTTATGAAGGATACGGACAG
ACAGAGTGCACTGCCGGGTGCTGCCTAACCATGCCTGGAGACTGGACCGCAGGCCATGTT
GGGGCCCCGATGCCGTGCAATTTGATAAAACTTGTTGATGTGGAAGAAATGAATTACATG
GCTGCCGAGGGCGAGGGCGAGGTGTGTGTGAAAGGGCCAAATGTATTTCAGGGCTACTTG
AAGGACCCAGCGAAAACAGCAGAAGCTTTGGACAAAGACGGCTGGTTACACACAGGGGAC
ATTGGAAAATGGTTACCAAATGGCACCTTGAAAATTATCGACCGGAAAAAGCACATATTT
AAGCTGGCACAAGGAGAATACATAGCCCCTGAAAAGATTGAAAATATCTACATGCGAAGT
GAGCCTGTTGCTCAGGTGTTTGTCCACGGAGAAAGCCTGCAGGCATTTCTCATTGCAATT
GTGGTACCAGATGTTGAGACATTATGTTCCTGGGCCCAAAAGAGAGGATTTGAAGGGTCG
TTTGAGGAACTGTGCAGAAATAAGGATGTCAAAAAAGCTATCCTCGAAGATATGGTGAGA
CTTGGGAAGGATTCTGGTCTGAAACCATTTGAACAGGTCAAAGGCATCACATTGCACCCT
GAATTATTTTCTATCGACAATGGCCTTCTGACTCCAACAATGAAGGCGAAAAGGCCAGAG
CTGCGGAACTATTTCAGGTCGCAGATAGATGACCTCTATTCCACTATCAAGGTTTAG
Enzyme 1 GenBank Gene ID D10040 Link Image
Enzyme 1 GeneCard ID ACSL1 Link Image
Enzyme 1 GenAtlas ID ACSL1 Link Image
Enzyme 1 HGNC ID HGNC:3569 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q34-q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Abe T, Fujino T, Fukuyama R, Minoshima S, Shimizu N, Toh H, Suzuki H, Yamamoto T: Human long-chain acyl-CoA synthetase: structure and chromosomal location. J Biochem (Tokyo). 1992 Jan;111(1):123-8. [PubMed Link Image]
  2. Ghosh B, Barbosa E, Singh I: Molecular cloning and sequencing of human palmitoyl-CoA ligase and its tissue specific expression. Mol Cell Biochem. 1995 Oct 4;151(1):77-81. [PubMed Link Image]
  3. Malhotra KT, Malhotra K, Lubin BH, Kuypers FA: Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors. Biochem J. 1999 Nov 15;344 Pt 1:135-43. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available