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Human Metabolome Database Version 2.5

 

Showing metabocard for 20-Hydroxyeicosatetraenoic acid (HMDB05998)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-04-12 20:56:15
Update Date 2011-06-09 10:24:34
Accession Number HMDB05998
Secondary Accession Numbers Not Available
Common Name 20-Hydroxyeicosatetraenoic acid
Description 20-Hydroxyeicosatetraenoic acid (20-HETE) is a metabolite of arachidonic acid. Cytochrome P450 enzymes of the 4A and 4F families catalyze the omega-hydroxylation of arachidonic acid and produce 20-HETE. 20-HETE is a potent constrictor or renal, cerebral and mesenteric arteries. The vasoconstrictor response to 20-HETE is associated with activation of protein kinase, Rho kinase and the mitogen activated protein (MAP) kinase pathway C. 20-HETE also increases intracellular Ca2+ by causing the depolarization of vascular smooth muscle membrane secondary to blocking the large-conductance Ca2+-activated K+-channels and by a direct effect on L-type Ca channels. Elevations in the production of 20-HETE mediate the myogenic response of skeletal, renal and cerebral arteries to elevations in transmural pressure. There is an important interaction between nitric oxide (NO) and the formation of 20-HETE production. NO inhibits the formation of 20-HETE formation in renal and cerebral arteries and that a fall in levels of 20-HETE contributes the cyclic GMP-independent dilator effect of NO to activate the large-conductance Ca2+-activated K+-channels and to dilate the cerebral arteries. (PMID: 16258232)
Synonyms
  1. 20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid
  2. 20-hydroxy-5,8,11,14-eicosatetraenoic acid
  3. 20-Hydroxyicosatetraenoic acid
  4. 20-Hydroxyarachidonic acid
  5. 20-Hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoic acid
  6. 20-Hydroxy arachidonic acid
  7. 20-HETE
  8. (all-Z)-20-hydroxy-5,8,11,14-Eicosatetraenoic acid
  9. (5Z,8Z,11Z,14Z)-20-Hydroxyicosa-5,8,11,14-tetraenoic acid
  10. 20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoate
  11. 20-hydroxy-5,8,11,14-eicosatetraenoate
  12. 20-Hydroxyicosatetraenoate
  13. 20-Hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
  14. (all-Z)-20-hydroxy-5,8,11,14-Eicosatetraenoate
  15. (5Z,8Z,11Z,14Z)-20-Hydroxyicosa-5,8,11,14-tetraenoate
Chemical IUPAC Name (5Z,8Z,11Z,14Z)-20-hydroxyicosa-5,8,11,14-tetraenoic acid
Chemical Formula C20H32O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Hydroxyeicosapolyenoic acids
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • carboxylic acid
  • alkene
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 320.466
Monoisotopic Molecular Weight 320.235138
Isomeric SMILES OCCCCCC=C/CC=C/CC=C/CC=C/CCCC(O)=O
Canonical SMILES OCCCCCC=CCC=CCC=CCC=CCCCC(O)=O
KEGG Compound ID C14748 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB05998 Link Image
Metagene Link HMDB05998 Link Image
METLIN ID Not Available
PubChem Compound 5283157 Link Image
PubChem Substance 17395746 Link Image
ChEBI ID 34306 Link Image
CAS Registry Number 79551-86-3
InChI Identifier InChI=1/C20H32O3/c21-19-17-15-13-11-9-7-5-3-1-2-4-6-8-10-12-14-16-18-20(22)23/h1,3-4,6-7,9-10,12,21H,2,5,8,11,13-19H2,(H,22,23)/b3-1-,6-4-,9-7-,12-10-
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.19e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5.87 [Predicted by ALOGPS]; 5.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.00301 +/- 0.00193 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Oxygenated lipids were quantified by Theresa L. Pedersen and John W. Newman at the USDA’s Western Human Nutrition Research Center, Davis, CA, and Lipomics Technologies, Inc.
References
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid Blood
Value 0.0014 (0.00043-0.0053) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Minuz P, Jiang H, Fava C, Turolo L, Tacconelli S, Ricci M, Patrignani P, Morganti A, Lechi A, McGiff JC: Altered release of cytochrome p450 metabolites of arachidonic acid in renovascular disease. Hypertension. 2008 May;51(5):1379-85. Epub 2008 Mar 31. [PubMed Link Image]
Biofluid CSF
Value 0.00037 +/- 0.00015 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Measured via MS/MS techniques from 4 pooled CSF samples provided by TNO/NuGO – The Netherlands
References
  • John W. Newman, USDA ARS Western Human Nutrition Research Center, Davis CA (personal communication - March 2, 2009)
Biofluid Urine
Value 0.0001 +/- 0.000019 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Barden A, Zilkens RR, Croft K, Mori T, Burke V, Beilin LJ, Puddey IB: A reduction in alcohol consumption is associated with reduced plasma F2-isoprostanes and urinary 20-HETE excretion in men. Free Radic Biol Med. 2007 Jun 1;42(11):1730-5. Epub 2007 Mar 12. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.0037 (0.0013-0.0059) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Minuz P, Jiang H, Fava C, Turolo L, Tacconelli S, Ricci M, Patrignani P, Morganti A, Lechi A, McGiff JC: Altered release of cytochrome p450 metabolites of arachidonic acid in renovascular disease. Hypertension. 2008 May;51(5):1379-85. Epub 2008 Mar 31. [PubMed Link Image]
Biofluid Blood
Value 0.0028 (0.0012-0.0067) uM
Age Adult:>18 yrs old
Sex Both
Condition Hypertension
Comments Not Available
References
  • Minuz P, Jiang H, Fava C, Turolo L, Tacconelli S, Ricci M, Patrignani P, Morganti A, Lechi A, McGiff JC: Altered release of cytochrome p450 metabolites of arachidonic acid in renovascular disease. Hypertension. 2008 May;51(5):1379-85. Epub 2008 Mar 31. [PubMed Link Image]
Biofluid CSF
Value 0.009 +/-0.23 uM
Age Adult:>18 yrs old
Sex Both
Condition Cerebral vasospasm
Comments Symptomatic cerebral vasospasm after subarachnoid hemorrhage
References
  • Poloyac SM, Reynolds RB, Yonas H, Kerr ME: Identification and quantification of the hydroxyeicosatetraenoic acids, 20-HETE and 12-HETE, in the cerebrospinal fluid after subarachnoid hemorrhage. J Neurosci Methods. 2005 Jun 15;144(2):257-63. Epub 2004 Dec 30. [PubMed Link Image]
Biofluid Urine
Value 0.0045 (0.0015-0.0087) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Minuz P, Jiang H, Fava C, Turolo L, Tacconelli S, Ricci M, Patrignani P, Morganti A, Lechi A, McGiff JC: Altered release of cytochrome p450 metabolites of arachidonic acid in renovascular disease. Hypertension. 2008 May;51(5):1379-85. Epub 2008 Mar 31. [PubMed Link Image]
Associated Disorders
Condition References
Cerebral vasospasm
  • Poloyac SM, Reynolds RB, Yonas H, Kerr ME: Identification and quantification of the hydroxyeicosatetraenoic acids, 20-HETE and 12-HETE, in the cerebrospinal fluid after subarachnoid hemorrhage. J Neurosci Methods. 2005 Jun 15;144(2):257-63. Epub 2004 Dec 30. [PubMed Link Image]
Hypertension
  • Minuz P, Jiang H, Fava C, Turolo L, Tacconelli S, Ricci M, Patrignani P, Morganti A, Lechi A, McGiff JC: Altered release of cytochrome p450 metabolites of arachidonic acid in renovascular disease. Hypertension. 2008 May;51(5):1379-85. Epub 2008 Mar 31. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References Not Available
Metabolic Enzymes
  1. Cytochrome P450 4A11
  2. Leukotriene-B(4) omega-hydroxylase 2
  3. Cytochrome P450 4A22
Enzyme 1 [top]
Enzyme 1 ID 5638
Enzyme 1 Name Cytochrome P450 4A11
Enzyme 1 Synonyms
  1. 20-hydroxyeicosatetraenoic acid synthase
  2. 20-HETE synthase
  3. CYP4AII
  4. CYPIVA11
  5. Cytochrome P-450HK-omega
  6. Cytochrome P450HL-omega
  7. Fatty acid omega-hydroxylase
  8. Lauric acid omega-hydroxylase
Enzyme 1 Gene Name CYP4A11
Enzyme 1 Protein Sequence >Cytochrome P450 4A11 
MSVSVLSPSRLLGDVSGILQAASLLILLLLLIKAVQLYLHRQWLLKALQQFPCPPSHWLF
GHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSY
RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQD
SPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQND
TIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKM
ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAS
ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHH
NPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL
LPDPTRIPIPIARLVLKSKNGIHLRLRRLPNPCEDKDQL
Enzyme 1 Number of Residues 519
Enzyme 1 Molecular Weight 59347.3
Enzyme 1 Theoretical pI 8.99
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in monooxygenase activity
Enzyme 1 Specific Function Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate, myristate and palmitate. Has little activity toward prostaglandins A1 and E1. Oxidizes arachidonic acid to 20-hydroxyeicosatetraenoic acid (20-HETE)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O [RN:R02879]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q02928 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CP4AB_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1560 bp 
ATGAGTGTCTCTGTGCTGAGCCCCAGCAGACTCCTGGGTGATGTCTCTGGAATCCTCCAA
GCGGCCTCCCTGCTCATTCTGCTTCTGCTGCTGATCAAGGCAGTTCAGCTCTACCTGCAC
AGGCAGTGGCTGCTCAAAGCCCTCCAGCAGTTCCCGTGCCCTCCCTCCCACTGGCTCTTC
GGGCACATCCAGGAGCTCCAACAGGACCAGGAGCTACAACGGATTCAGAAATGGGTGGAG
ACATTCCCAAGTGCCTGTCCTCATTGGCTATGGGGAGGCAAAGTTCGTGTCCAGCTCTAT
GACCCTGACTATATGAAGGTGATTCTGGGGAGATCAGACCCGAAATCCCATGGTTCCTAC
AGATTCCTGGCTCCATGGATTGGGTACGGCTTGCTCCTGTTGAATGGGCAGACATGGTTC
CAGCATCGACGGATGCTGACCCCAGCCTTCCACTATGACATCCTGAAGCCCTATGTGGGG
CTCATGGCAGACTCTGTACGAGTGATGCTGGACAAATGGGAAGAGCTCCTTGGCCAGGAT
TCCCCTCTGGAGGTCTTTCAGCACGTCTCCTTGATGACCCTGGACACCATCATGAAGTGT
GCCTTCAGCCATCAGGGCAGCATCCAGGTGGACAGGAATTCTCAGTCCTACATACAGGCC
ATTAGTGACCTGAACAACCTGGTTTTTTCCCGTGTGAGGAATGCCTTTCACCAGAATGAC
ACCATCTACAGCCTGACCTCTGCTGGCCGCTGGACACACCGCGCCTGCCAGCTGGCCCAT
CAGCACACAGACCAAGTGATCCAACTGAGGAAGGCTCAACTACAGAAGGAGGGGGAGCTG
GAGAAGATCAAGAGGAAGAGGCATTTGGATTTTCTGGATATCCTCCTCTTGGCCAAAATG
GAGAATGGGAGCATCTTGTCAGACAAGGACCTCCGTGCTGAGGTGGACACGTTCATGTTT
GAGGGCCACGACACCACAGCCAGTGGGATCTCCTGGATCCTCTATGCTCTGGCCACACAC
CCCAAGCATCAGGAGAGGTGCCGGGAGGAGATCCACAGCCTCCTGGGTGATGGAGCCTCC
ATCACCTGGAACCACCTGGACCAGATGCCCTACACCACCATGTGCATTAAGGAGGCACTG
AGGCTCTACCCACCGGTGCCAGGCATTGGCAGAGAGCTCAGCACTCCCGTCACCTTCCCT
GATGGGCGCTCCTTGCCCAAAGGTATCATGGTCCTCCTCTCCATTTATGGCCTTCACCAC
AACCCAAAAGTGTGGCCCAACCCAGAGGTGTTTGACCCTTTCCGTTTTGCACCGGGTTCT
GCTCAACACAGCCACGCTTTCCTGCCCTTCTCAGGAGGATCAAGGAACTGCATTGGGAAA
CAATTTGCCATGAACGAGCTGAAGGTGGCCACGGCCCTGACCCTGCTCCGCTTTGAGCTG
CTGCCTGATCCCACCAGGATCCCCATCCCCATTGCACGACTTGTGTTGAAATCCAAAAAT
GGAATCCACCTGCGTCTCAGGAGGCTCCCTAACCCTTGTGAAGACAAGGACCAGCTTTGA
Enzyme 1 GenBank Gene ID L04751 Link Image
Enzyme 1 GeneCard ID CYP4A11 Link Image
Enzyme 1 GenAtlas ID CYP4A11 Link Image
Enzyme 1 HGNC ID HGNC:2642 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Palmer CN, Richardson TH, Griffin KJ, Hsu MH, Muerhoff AS, Clark JE, Johnson EF: Characterization of a cDNA encoding a human kidney, cytochrome P-450 4A fatty acid omega-hydroxylase and the cognate enzyme expressed in Escherichia coli. Biochim Biophys Acta. 1993 Feb 20;1172(1-2):161-6. [PubMed Link Image]
  2. Kawashima H, Kusunose E, Kikuta Y, Kinoshita H, Tanaka S, Yamamoto S, Kishimoto T, Kusunose M: Purification and cDNA cloning of human liver CYP4A fatty acid omega-hydroxylase. J Biochem (Tokyo). 1994 Jul;116(1):74-80. [PubMed Link Image]
  3. Imaoka S, Ogawa H, Kimura S, Gonzalez FJ: Complete cDNA sequence and cDNA-directed expression of CYP4A11, a fatty acid omega-hydroxylase expressed in human kidney. DNA Cell Biol. 1993 Dec;12(10):893-9. [PubMed Link Image]
  4. Bellamine A, Wang Y, Waterman MR, Gainer JV 3rd, Dawson EP, Brown NJ, Capdevila JH: Characterization of the CYP4A11 gene, a second CYP4A gene in humans. Arch Biochem Biophys. 2003 Jan 1;409(1):221-7. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. 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]
  7. Kawashima H, Kusunose E, Kubota I, Maekawa M, Kusunose M: Purification and NH2-terminal amino acid sequences of human and rat kidney fatty acid omega-hydroxylases. Biochim Biophys Acta. 1992 Jan 24;1123(2):156-62. [PubMed Link Image]
  8. Bell DR, Plant NJ, Rider CG, Na L, Brown S, Ateitalla I, Acharya SK, Davies MH, Elias E, Jenkins NA, et al.: Species-specific induction of cytochrome P-450 4A RNAs: PCR cloning of partial guinea-pig, human and mouse CYP4A cDNAs. Biochem J. 1993 Aug 15;294 ( Pt 1):173-80. [PubMed Link Image]
  9. Hoch U, Ortiz De Montellano PR: Covalently linked heme in cytochrome p4504a fatty acid hydroxylases. J Biol Chem. 2001 Apr 6;276(14):11339-46. Epub 2001 Jan 3. [PubMed Link Image]
  10. LeBrun LA, Hoch U, Ortiz de Montellano PR: Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family. J Biol Chem. 2002 Apr 12;277(15):12755-61. Epub 2002 Jan 30. [PubMed Link Image]
  11. Gainer JV, Bellamine A, Dawson EP, Womble KE, Grant SW, Wang Y, Cupples LA, Guo CY, Demissie S, O'Donnell CJ, Brown NJ, Waterman MR, Capdevila JH: Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension. Circulation. 2005 Jan 4;111(1):63-9. Epub 2004 Dec 20. [PubMed Link Image]
  12. Cho BH, Park BL, Kim LH, Chung HS, Shin HD: Highly polymorphic human CYP4A11 gene. J Hum Genet. 2005;50(5):259-63. Epub 2005 May 14. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6302
Enzyme 2 Name Leukotriene-B(4) omega-hydroxylase 2
Enzyme 2 Synonyms
  1. CYPIVF3
  2. Cytochrome P450 4F3
  3. Cytochrome P450-LTB-omega
  4. Leukotriene-B(4) 20-monooxygenase 2
Enzyme 2 Gene Name CYP4F3
Enzyme 2 Protein Sequence >Leukotriene-B(4) omega-hydroxylase 2 
MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWF
LGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPK
DKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQL
LASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQIL
LYIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFID
VLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQE
LLKDREPKEIEWDDLAQLPFLTMCIKESLRLHPPVPAVSRCCTQDIVLPDGRVIPKGIIC
LISVFGTHHNPAVWPDPEVYDPFRFDPKNIKERSPLAFIPFSAGPRNCIGQAFAMAEMKV
VLGLTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS
Enzyme 2 Number of Residues 520
Enzyme 2 Molecular Weight 59846.1
Enzyme 2 Theoretical pI 7.68
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 2 General Function Involved in monooxygenase activity
Enzyme 2 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. This enzyme requires molecular oxygen and NADPH for the omega-hydroxylation of LTB4, a potent chemoattractant for polymorphonuclear leukocytes
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + H+ + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14- tetraenoate + NADP+ + H2O [RN:R03866]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 11-31
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3123723 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q08477 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CP4F3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1563 bp 
ATGCCACAGCTGAGCCTGTCCTCGCTGGGCCTTTGGCCAATGGCAGCATCCCCGTGGCTG
CTCCTGCTGCTGGTTGGGGCCTCCTGGCTCCTGGCCCGCATCCTGGCCTGGACCTATACC
TTCTATGACAACTGCTGCCGCCTCCGGTGTTTCCCGCAACCCCCGAAACGGAATTGGTTC
TTGGGTCACCTGGGCCTGATTCACAGCTCGGAGGAAGGTCTCCTATACACACAAAGCCTG
GCATGCACCTTCGGTGATATGTGCTGCTGGTGGGTGGGGCCCTGGCACGCAATCGTCCGC
ATCTTCCACCCCACCTACATCAAGCCTGTGCTCTTTGCTCCAGCTGCCATTGTACCAAAG
GACAAGGTCTTCTACAGCTTCCTGAAGCCCTGGCTGGGGGATGGGCTCCTGCTGAGTGCT
GGTGAAAAGTGGAGCCGCCACCGTCGGATGCTGACGCCTGCCTTCCATTTCAACATCCTG
AAGCCCTATATGAAGATTTTCAATGAGAGTGTGAACATCATGCATGCCAAGTGGCAGCTC
CTGGCCTCAGAGGGTAGTGCCCGTCTGGACATGTTTGAGCACATCAGCCTCATGACCTTG
GACAGTCTGCAGAAATGTGTCTTCAGCTTTGACAGCCATTGCCAGGAGAAGCCCAGTGAA
TATATTGCCGCCATCTTGGAGCTCAGTGCCCTTGTGACAAAAAGACACCAGCAGATCCTC
CTGTACATAGACTTCCTGTATTATCTCACCCCTGATGGGCAGCGTTTCCGCAGGGCCTGC
CGCCTGGTGCACGACTTCACAGATGACGTCATCCAGGAGCGGCGCCGCACCCTCCCTAGC
CAGGGTGTTGATGACTTCCTCCAAGCCAAGGCCAAATCCAAGACTTTGGACTTCATTGAT
GTACTCCTGCTGAGCAAGGATGAAGATGGGAAGAAGTTGTCCGATGAGGACATAAGAGCA
GAAGCTGACACCTTTATGTTTGAGGGCCATGACACCACAGCCAGTGGTCTCTCCTGGGTC
CTGTACCACCTTGCAAAGCACCCGGAATACCAGGAGCGCTGTCGGCAGGAGGTACAAGAG
CTTCTGAAGGACCGTGAGCCTAAAGAGATTGAATGGGACGACCTGGCCCAGCTGCCCTTC
CTGACCATGTGCATTAAGGAGAGCCTGAGGCTGCATCCCCCAGTCCCTGCCGTCTCTCGC
TGCTGCACCCAAGACATTGTGCTCCCAGACGGCCGGGTCATCCCCAAAGGCATTATCTGC
CTCATCAGTGTTTTTGGAACCCATCACAACCCAGCCGTGTGGCCGGACCCTGAGGTCTAT
GACCCCTTTCGCTTTGACCCAAAGAACATCAAGGAGAGGTCACCTCTGGCTTTTATTCCC
TTCTCAGCAGGGCCCAGGAACTGCATCGGGCAGGCGTTCGCGATGGCGGAGATGAAGGTG
GTCCTGGGGCTCACGCTGCTGGCCTTCCGCGTCCTGCCTGACCACACCGAGCCCCGCAGG
AAGCCGGAGCTGGTCCTGCGCGCAGAGGGCGGACTTTGGCTGCGGGTGGAGCCCCTGAGC
TGA
Enzyme 2 GenBank Gene ID AB002454 Link Image
Enzyme 2 GeneCard ID CYP4F3 Link Image
Enzyme 2 GenAtlas ID CYP4F3 Link Image
Enzyme 2 HGNC ID HGNC:2646 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 19p13.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kikuta Y, Kusunose E, Endo K, Yamamoto S, Sogawa K, Fujii-Kuriyama Y, Kusunose M: A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase. J Biol Chem. 1993 May 5;268(13):9376-80. [PubMed Link Image]
  2. Kikuta Y, Kato M, Yamashita Y, Miyauchi Y, Tanaka K, Kamada N, Kusunose M: Human leukotriene B4 omega-hydroxylase (CYP4F3) gene: molecular cloning and chromosomal localization. DNA Cell Biol. 1998 Mar;17(3):221-30. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 12893
Enzyme 3 Name Cytochrome P450 4A22
Enzyme 3 Synonyms
  1. CYPIVA22
  2. Fatty acid omega-hydroxylase
  3. Lauric acid omega-hydroxylase
Enzyme 3 Gene Name CYP4A22
Enzyme 3 Protein Sequence >Cytochrome P450 4A22 
MSVSVLSPSRRLGGVSGILQVTSLLILLLLLIKAAQLYLHRQWLLKALQQFPCPPSHWLF
GHIQEFQHDQELQRIQERVKTFPSACPYWIWGGKVRVQLYDPDYMKVILGRSDPKSHGSY
KFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHNDILKPYVGLMADSVRVMLDKWEELLGQD
SPLEVFQHVSLMTLDTIMKSAFSHQGSIQVDRNSQSYIQAISDLNSLVFCCMRNAFHEND
TIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKM
ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHGLLGDGAS
ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHH
NPKVWPNLEVFDPSRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNQLKVARALTLLRFEL
LPDPTRIPIPMARLVLKSKNGIHLRLRRLPNPCEDKDQL
Enzyme 3 Number of Residues 519
Enzyme 3 Molecular Weight 59245.3
Enzyme 3 Theoretical pI 9.40
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 3 General Function Involved in monooxygenase activity
Enzyme 3 Specific Function Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate and palmitate. Shows no activity towards arachidonic acid and prostaglandin A1. Lacks functional activity in the kidney and does not contribute to renal 20-hydroxyeicosatetraenoic acid (20-HETE) biosynthesis
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O [RN:R02879]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 8571055 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q5TCH4 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CP4AM_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1560 bp 
ATGAGTGTCTCTGTCCTGAGCCCCAGCAGACGCCTGGGTGGTGTCTCCGGGATCCTCCAA
GTGACCTCCCTGCTCATTCTGCTTCTGCTGCTGATCAAGGCAGCTCAGCTCTACCTGCAT
AGGCAGTGGCTGCTCAAAGCCCTCCAGCAGTTCCCGTGCCCTCCCTCCCACTGGCTCTTC
GGGCACATCCAGGAGTTCCAACACGACCAGGAGCTACAACGGATTCAGGAACGGGTGAAG
ACATTCCCAAGTGCCTGTCCTTATTGGATATGGGGAGGCAAAGTTCGTGTCCAGCTCTAT
GACCCTGACTATATGAAGGTGATTCTGGGGAGATCAGACCCGAAATCCCATGGTTCCTAC
AGATTCCTGGCTCCACGGATTGGGTACGGCTTGCTCCTGTTGAATGGGCAGACATGGTTC
CAGCATCGACGGATGCTGACCCCAGCCTTCCACAATGACATCCTGAAGCCATATGTGGGG
CTCATGGCAGACTCTGTACGAGTGATGCTGGACAAATGGGAAGAGCTCCTTGGCCAGGAT
TCCCCTCTGGAGGTCTTTCAGCACGTCTCCTTGATGACCCTGGACACCATCATGAAGAGT
GCCTTCAGCCATCAGGGCAGCATCCAGGTGGACAGGAATTCTCAGTCCTACATCCAGGCC
ATTAGTGACCTGAACAGCCTGGTTTTTTGCTGTATGAGGAATGCCTTTCATGAGAATGAC
ACCATCTACAGCCTGACCTCTGCTGGCCGCTGGACACACCGCGCCTGCCAGCTGGCCCAT
CAGCACACAGACCAAGTGATCCAACTGAGGAAGGCTCAACTACAGAAGGAGGGGGAGCTG
GAGAAGATCAAGAGGAAGAGGCACTTGGATTTTCTGGACATCCTCCTCTTGGCCAAAATG
GAGAATGGGAGCATCTTGTCAGACAAGGACCTCCGTGCTGAGGTGGACACGTTCATGTTT
GAGGGCCACGACACCACAGCCAGTGGGATCTCCTGGATCCTCTATGCTCTGGCCACACAC
CCCAAGCATCAGGAGAGGTGCCGGGAGGAGATCCATGGCCTCCTGGGTGATGGAGCCTCC
ATCACCTGGAACCACCTGGACCAGATGCCCTACACCACCATGTGCATTAAGGAGGCACTG
AGGCTCTACCCACCGGTGCCAGGCATTGGAAGAGAGCTCAGCACTCCCGTCACCTTCCCT
GATGGGCGCTCCTTGCCCAAAGGTATCATGGTCCTCCTCTCCATTTATGGCCTTCACCAC
AACCCAAAAGTGTGGCCCAACCTAGAGGTGTTTGACCCTTCCCGTTTTGCACCGGGTTCT
GCTCAACACAGCCACGCTTTCCTGCCCTTCTCAGGAGGATCAAGGAACTGCATCGGGAAA
CAATTTGCCATGAACCAGCTGAAGGTGGCCAGGGCCCTGACCCTGCTCCGCTTTGAGCTG
CTGCCTGATCCCACCAGGATCCCCATCCCCATTGCACGACTTGTGTTGAAATCCAAAAAT
GGAATCCACCTGCGTCTCAGGAGGCTCCCTAACCCTTGTGAAGACAAGGACCAGCTTTGA
Enzyme 3 GenBank Gene ID AF208532 Link Image
Enzyme 3 GeneCard ID CYP4A22 Link Image
Enzyme 3 GenAtlas ID CYP4A22 Link Image
Enzyme 3 HGNC ID HGNC:20575 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p33
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Kawashima H, Naganuma T, Kusunose E, Kono T, Yasumoto R, Sugimura K, Kishimoto T: Human fatty acid omega-hydroxylase, CYP4A11: determination of complete genomic sequence and characterization of purified recombinant protein. Arch Biochem Biophys. 2000 Jun 15;378(2):333-9. [PubMed Link Image]
  2. Gainer JV, Bellamine A, Dawson EP, Womble KE, Grant SW, Wang Y, Cupples LA, Guo CY, Demissie S, O'Donnell CJ, Brown NJ, Waterman MR, Capdevila JH: Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension. Circulation. 2005 Jan 4;111(1):63-9. Epub 2004 Dec 20. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. 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]
  5. Hiratsuka M, Nozawa H, Katsumoto Y, Moteki T, Sasaki T, Konno Y, Mizugaki M: Genetic polymorphisms and haplotype structures of the CYP4A22 gene in a Japanese population. Mutat Res. 2006 Jul 25;599(1-2):98-104. Epub 2006 Jun 27. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available