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Human Metabolome Database Version 2.5

 

Showing metabocard for 20-Hydroxy-leukotriene B4 (HMDB01509)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-01-20 10:34:45
Accession Number HMDB01509
Secondary Accession Numbers HMDB05092
Common Name 20-Hydroxy-leukotriene B4
Description 20-hydroxy- Leukotriene B4 (20-OH-LTB4) is an omega-hydroxylated metabolite of leukotriene B4 in human neutrophils. Elevated urinary concentrations of 20-OH-LTB4 and LTB4 are found in patients with Sjogren-Larsson syndrome (SLS, OMIM 270220), an autosomal recessively inherited neurocutaneous disorder caused by a deficiency of the microsomal enzyme fatty aldehyde dehydrogenase (FALDH), which as an essential role in LTB4 metabolism. Preterm birth seems to be one of the features of the syndrome. The reason for the preterm birth is unclear. It is hypothesized that it relates to the defective LTB4 degradation in SLS. The pathological urinary excretion of LTB4 and 20-OH-LTB4 is a biochemical marker for SLS. Surprisingly, 20-OH-LTB4 concentrations are normal in CSF. Leukotriene B4 is the major metabolite in neutrophil polymorphonuclear leukocytes. Leukotrienes are metabolites of arachidonic acid derived from the action of 5-LO (5-lipoxygenase). The immediate product of 5-LO is LTA4 (leukotriene A4), which is enzymatically converted into either LTB4 (leukotriene B4) by LTA4 hydrolase or LTC4 (leukotriene C4) by LTC4 synthase. The regulation of leukotriene production occurs at various levels, including expression of 5-LO, translocation of 5-LO to the perinuclear region and phosphorylation to either enhance or inhibit the activity of 5-LO. Biologically active LTB4 is metabolized by w-oxidation carried out by specific cytochrome P450s (CYP4F) followed by beta-oxidation from the w-carboxy position and after CoA ester formation. Other specific pathways of leukotriene metabolism include the 12-hydroxydehydrogenase/ 15-oxo-prostaglandin-13-reductase that form a series of conjugated diene metabolites that have been observed to be excreted into human urine. Metabolism of LTC4 occurs by sequential peptide cleavage reactions involving a gamma-glutamyl transpeptidase that forms LTD4 (leukotriene D4) and a membrane-bound dipeptidase that converts LTD4 into LTE4 (leukotriene E4) before w-oxidation. These metabolic transformations of the primary leukotrienes are critical for termination of their biological activity, and defects in expression of participating enzymes may be involved in specific genetic disease. (PMID: 12709426, 9799565, 11408337, 17623009) Leukotrienes are eicosanoids. The eicosanoids consist of the prostaglandins (PGs), thromboxanes (TXs), leukotrienes (LTs) and lipoxins (LXs). The PGs and TXs are collectively identified as prostanoids. Prostaglandins were originally shown to be synthesized in the prostate gland, thromboxanes from platelets (thrombocytes) and leukotrienes from leukocytes, hence the derivation of their names. All mammalian cells except erythrocytes synthesize eicosanoids. These molecules are extremely potent, able to cause profound physiological effects at very dilute concentrations. All eicosanoids function locally at the site of synthesis, through receptor-mediated G-protein linked signaling pathways.
Synonyms
  1. (5S,12R)-5,12,20-Trihydroxy-(6Z,8E,10E,14Z)-eicosatetraenoic acid
  2. (5S,6Z,8E,10E,12R,14Z)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoic acid
  3. (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-Trihydroxyeicosa-6,8,10,14-tetraenoate
  4. (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-Trihydroxyicosa-6,8,10,14-tetraenoate
  5. 20-hydroxy LTB4
  6. 20-Hydroxy-leukotriene B4
  7. 20-Hydroxy-LTB4
  8. 20-hydroxyleukotriene B4
  9. 20-OH-Leukotriene B4
  10. 20-OH-LTB4
  11. 5S,12R,20-trihydroxy-6Z,8E,10E,14Z-eicosatetraenoic acid
  12. omega-Hydroxy-LTB4
  13. w-Hydroxy-LTB4
  14. [S-[R*,S*-(E,Z,E,Z)]]-5,12,20-trihydroxy-6,8,10,14-Eicosatetraenoic acid
  15. (5S,12R)-5,12,20-Trihydroxy-(6Z,8E,10E,14Z)-eicosatetraenoate
  16. (5S,6Z,8E,10E,12R,14Z)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate
  17. (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-Trihydroxyeicosa-6,8,10,14-tetraenoic acid
  18. (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-Trihydroxyicosa-6,8,10,14-tetraenoic acid
  19. 5S,12R,20-trihydroxy-6Z,8E,10E,14Z-eicosatetraenoate
  20. [S-[R*,S*-(E,Z,E,Z)]]-5,12,20-trihydroxy-6,8,10,14-Eicosatetraenoate
  21. 5,12,20-TriHETE
  22. 5,12,20-THETE
  23. 20-OH-5S,12S-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoic acid
  24. 20-OH-5S,12S-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoate
Chemical IUPAC Name Not Available
Chemical Formula C20H32O5
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Leukotrienes
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • carboxylic acid
  • alkene
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 352.465
Monoisotopic Molecular Weight 352.224976
Isomeric SMILES OCCCCCC=C/C[C@@H](O)C=CC=CC=C/[C@@H](O)CCCC(O)=O
Canonical SMILES OCCCCCC=CCC(O)C=CC=CC=CC(O)CCCC(O)=O
KEGG Compound ID C04853 Link Image
BioCyc ID 20-OH-LTB4 Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB01509 Link Image
Metagene Link HMDB01509 Link Image
METLIN ID 6287 Link Image
PubChem Compound 5280745 Link Image
PubChem Substance 7409 Link Image
ChEBI ID 15646 Link Image
CAS Registry Number 79516-82-8
InChI Identifier InChI=1/C20H32O5/c21-17-10-6-2-1-3-7-12-18(22)13-8-4-5-9-14-19(23)15-11-16-20(24)25/h3-5,7-9,13-14,18-19,21-23H,1-2,6,10-12,15-17H2,(H,24,25)/b5-4+,7-3-,13-8+,14-9-/t18-,19-/m1/s1
Synthesis Reference Zamboni, Robert; Rokach, Joshua. Stereospecific synthesis of two metabolites of LTB4. Tetrahedron Letters (1982), 23(46), 4751-4.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.033 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Liquid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 2.7 [Predicted by PubChem via XLOGP]; 4.22 [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
  • Membrane (Predicted from LogP)
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid CSF
Value 0.0000075 (0.0 - 0.000015) uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Willemsen MA, Rotteveel JJ, de Jong JG, Wanders RJ, IJlst L, Hoffmann GF, Mayatepek E: Defective metabolism of leukotriene B4 in the Sjogren-Larsson syndrome. J Neurol Sci. 2001 Jan 15;183(1):61-7. [PubMed Link Image]
Biofluid Urine
Value 0.0000025 (0.0 - 0.000005) umol/mmol creatinine
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Willemsen MA, Rotteveel JJ, de Jong JG, Wanders RJ, IJlst L, Hoffmann GF, Mayatepek E: Defective metabolism of leukotriene B4 in the Sjogren-Larsson syndrome. J Neurol Sci. 2001 Jan 15;183(1):61-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Urine
Value 0.0003 +/- 0.00014 umol/mmol creatinine
Age Children:1-13 yrs old
Sex N/A
Condition Sjögren-Larsson syndrome
Comments Not Available
References
  • Willemsen MA, Rotteveel JJ, de Jong JG, Wanders RJ, IJlst L, Hoffmann GF, Mayatepek E: Defective metabolism of leukotriene B4 in the Sjogren-Larsson syndrome. J Neurol Sci. 2001 Jan 15;183(1):61-7. [PubMed Link Image]
Associated Disorders
Condition References
Sjögren-Larsson syndrome
  • Willemsen MA, Rotteveel JJ, de Jong JG, Wanders RJ, IJlst L, Hoffmann GF, Mayatepek E: Defective metabolism of leukotriene B4 in the Sjogren-Larsson syndrome. J Neurol Sci. 2001 Jan 15;183(1):61-7. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Willemsen MA, Rotteveel JJ, de Jong JG, Wanders RJ, IJlst L, Hoffmann GF, Mayatepek E: Defective metabolism of leukotriene B4 in the Sjogren-Larsson syndrome. J Neurol Sci. 2001 Jan 15;183(1):61-7. [PubMed Link Image]
  2. Goldman DW, Olson DM, Payan DG, Gifford LA, Goetzl EJ: Development of receptors for leukotriene B4 on HL-60 cells induced to differentiate by 1 alpha,25-dihydroxyvitamin D3. J Immunol. 1986 Jun 15;136(12):4631-6. [PubMed Link Image]
Metabolic Enzymes
  1. Leukotriene-B(4) omega-hydroxylase 1
  2. Leukotriene-B(4) omega-hydroxylase 2
Enzyme 1 [top]
Enzyme 1 ID 6301
Enzyme 1 Name Leukotriene-B(4) omega-hydroxylase 1
Enzyme 1 Synonyms
  1. CYPIVF2
  2. Cytochrome P450 4F2
  3. Cytochrome P450-LTB-omega
  4. Leukotriene-B(4) 20-monooxygenase 1
Enzyme 1 Gene Name CYP4F2
Enzyme 1 Protein Sequence >Leukotriene-B(4) omega-hydroxylase 1 
MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWF
WGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPK
DKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQL
LASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEIL
LHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFID
VLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQE
LLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIIC
LISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKV
VLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS
Enzyme 1 Number of Residues 520
Enzyme 1 Molecular Weight 59852.8
Enzyme 1 Theoretical pI 7.08
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 Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 1 Pathways
Enzyme 1 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 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4519535 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P78329 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CP4F2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1563 bp 
ATGTCCCAGCTGAGCCTGTCCTGGCTGGGCCTCGGGCCAGTGGCAGCATCCCCTTGGCTG
CTCCTCCTGCTGGTCGGGGCCTCCTGGCTCCTGGCCCATGTCCTGGCCTGGACCTACGCC
TTCTATGACAACTGCCGCCGCCTTCGGTGTTTCCCACAACCCCCGAGACGGAACTGGTTT
TGGGGACACCAGGGCATGGTCAACCCCACAGAGGAGGGCATGAGAGTTCTGACTCAGCTG
GTGGCCACCTACCCCCAGGGCTTTAAGGTCTGGATGGGACCCATCTCCCCCCTCCTCAGT
TTGTGCCACCCCGACATCATCCGGTCTGTCATCAACGCCTCAGCTGCCATTGCACCAAAG
GACAAGTTCTTCTACAGCTTCCTGGAGCCCTGGCTGGGGGATGGGCTCCTGCTGAGTGCT
GGTGACAAGTGGAGCCGCCACCGTCGGATGCTGACGCCTGCCTTCCATTTCAACATCCTG
AAGCCCTATATGAAGATTTTCAATGAGAGTGTGAACATCATGCACGCCAAGTGGCAGCTC
CTGGCCTCAGAGGGTAGTGCCTGTTTGGATATGTTTGAGCACATCAGCCTCATGACCTTG
GACAGTCTACAGAAATGTGTCTTCAGCTTTGACAGCCATTGTCAGGAGAAACCCAGTGAA
TATATTGCCGCCATCTTGGAGCTCAGTGCCCTTGTATCAAAAAGACACCATGAGATCCTC
CTGCATATTGACTTCCTGTATTATCTCACCCCTGATGGGCAGCGTTTCCGCAGGGCCTGC
CGCCTGGTGCACGACTTCACAGATGCCGTCATCCAGGAGCGGCGCCGCACTCTCCCTAGC
CAGGGTGTTGATGACTTCCTCCAAGCCAAGGCCAAATCCAAGACTTTGGACTTCATTGAT
GTACTCCTGCTGAGCAAGGATGAAGACGGGAAGAAGTTATCTGATGAGGACATAAGAGCA
GAAGCTGACACCTTTATGTTTGAGGGCCATGACACCACGGCCAGTGGTCTCTCCTGGGTC
CTGTACCACCTTGCAAAGCACCCAGAATACCAGGAGCGCTGCCGGCAGGAGGTGCAAGAA
CTTCTGAAGGACCGTGAGCCTAAAGAGATTGAATGGGACGACCTGGCCCATTTGCCCTTC
CTGACCATGTGCATGAAGGAGAGCCTGCGGCTGCATCCCCCAGTCCCGGTCATCTCCCGC
CATGTCACCCAGGACATTGTGCTCCCAGACGGCCGGGTCATCCCCAAAGGCATTATCTGC
CTCATCAGTGTTTTCGGAACCCATCACAACCCAGCTATGTGGCCGGACCCTGAGGTCTAC
GACCCCTTTCGCTTTGACCCAGAGAACATCAAGGAGAGGTCACCTCTGGCTTTTATTCCC
TTCTCGGCAGGGCCCAGGAACTGCATCGGGCAGACGTTCGCGATGGCGGAGATGAAGGTG
GTCCTGGCGCTCACGCTGCTGCGCTTCCGCGTCCTGCCTGACCACACCGAGCCCCGCAGG
AAGCCGGAGCTGGTCCTGCGCGCAGAGGGCGGACTTTGGCTGCGGGTGGAGCCCCTGAGC
TGA
Enzyme 1 GenBank Gene ID AB015306 Link Image
Enzyme 1 GeneCard ID CYP4F2 Link Image
Enzyme 1 GenAtlas ID CYP4F2 Link Image
Enzyme 1 HGNC ID HGNC:2645 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 19pter-p13.11
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kikuta Y, Kusunose E, Kondo T, Yamamoto S, Kinoshita H, Kusunose M: Cloning and expression of a novel form of leukotriene B4 omega-hydroxylase from human liver. FEBS Lett. 1994 Jul 4;348(1):70-4. [PubMed Link Image]
  2. Kikuta Y, Miyauchi Y, Kusunose E, Kusunose M: Expression and molecular cloning of human liver leukotriene B4 omega-hydroxylase (CYP4F2) gene. DNA Cell Biol. 1999 Sep;18(9):723-30. [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. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [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. Zhang X, Chen L, Hardwick JP: Promoter activity and regulation of the CYP4F2 leukotriene B(4) omega-hydroxylase gene by peroxisomal proliferators and retinoic acid in HepG2 cells. Arch Biochem Biophys. 2000 Jun 15;378(2):364-76. [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