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Human Metabolome Database Version 2.5

 

Showing metabocard for Leukotriene B4 (HMDB01085)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-29 14:35:04
Accession Number HMDB01085
Secondary Accession Numbers HMDB05072
Common Name Leukotriene B4
Description 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 b-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. The term leukotriene was coined to indicate the presence of three conjugated double bonds within the 20-carbon structure of arachidonic acid as well as the fact that these compounds were derived from leucocytes such as PMNNs or transformed mast cells. Interestingly, most of the cells known to express 5-LO are of myeloid origin, which includes neutrophils, eosinophils, mast cells, macrophages, basophils and monocytes. Leukotriene biosynthesis begins with the specific oxidation of arachidonic acid by a free radical mechanism as a consequence of interaction with 5-LO. The first enzymatic step involves the abstraction of a hydrogen atom from C-7 of arachidonate followed by the addition of molecular oxygen to form 5-HpETE (5-hydroperoxyeicosatetraenoic acid). A second enzymatic step is also catalysed by 5-LO and involves removal of a hydrogen atom from C-10, resulting in formation of the conjugated triene epoxide LTA4. LTA4 must then be released by 5-LO and encounter either LTA4-H (LTA4 hydrolase) or LTC4-S [LTC4 (leukotriene C4) synthase]. LTA4-H can stereospecifically add water to C-12 while retaining a specific double-bond geometry, leading to LTB4 [leukotriene B4, 5(S),12(R)-dihydroxy-6,8,10,14-(Z,E,E,Z)-eicosatetraenoic acid]. If LTA4 encounters LTC4-S, then the reactive epoxide is opened at C-6 by the thiol anion of glutathione to form the product LTC4 [5(S)-hydroxy-6(R)-S-glutathyionyl-7,9,11,14- (E,E,Z,Z)-eicosatetraenoic acid], essentially a glutathionyl adduct of oxidized arachidonic acid. Both of these terminal leukotrienes are biologically active in that specific GPCRs recognize these chemical structures and receptor recognition initiates complex intracellular signalling cascades. In order for these molecules to serve as lipid mediators, however, they must be released from the biosynthetic cell into the extracellular milieu so that they can encounter the corresponding GPCRs. Surprising features of this cascade include the recognition of the assembly of critical enzymes at the perinuclear region of the cell and even localization of 5-LO within the nucleus of some cells. Under some situations, the budding phagosome has been found to assemble these proteins. Non-enzymatic proteins such as FLAP are now known as critical partners of this protein-machine assembly. An unexpected pathway of leukotriene biosynthesis involves the transfer of the chemically reactive intermediate, LTA4, from the biosynthetic cell followed by conversion into LTB4 or LTC4 by other cells that do not express 5-LO. (PMID 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. (6z,8e,10e,14z)-(5s,12r)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate
  2. leukotriene B4 ethanol solution
  3. (6z,8e,10e,14z)-(5s,12r)-5,12-dihydroxyicosa-6,8,10,14-tetraenoic acid
  4. 5,12-DiHETE
  5. 5,12-dihydroxy-6,10-trans -8,14-cis -eicosatetraenoate
  6. 5,12-dihydroxy-6,10-trans -8,14-cis -eicosatetraenoic acid
Chemical IUPAC Name (5S,6Z,8E,10E,12R,14Z)-5,12-dihydroxyicosa-6,8,10,14-tetraenoic acid
Chemical Formula C20H32O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Leukotrienes
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • alkene
Biofunction
  • DNA component
  • Component of Prostaglandin and leukotriene metabolism
Application
Source
  • Endogenous
Average Molecular Weight 336.466
Monoisotopic Molecular Weight 336.230072
Isomeric SMILES CCCCCC=C/C[C@@H](O)C=CC=CC=C/[C@@H](O)CCCC(O)=O
Canonical SMILES CCCCCC=CCC(O)C=CC=CC=CC(O)CCCC(O)=O
KEGG Compound ID C02165 Link Image
BioCyc ID 6Z8E10E14Z-5S12R-512-DIHYDROXYI Link Image
BiGG ID 39243 Link Image
Wikipedia Link Leukotriene B4 Link Image
NuGOwiki Link HMDB01085 Link Image
Metagene Link HMDB01085 Link Image
METLIN ID 406 Link Image
PubChem Compound 5280492 Link Image
PubChem Substance 10440505 Link Image
ChEBI ID 15647 Link Image
CAS Registry Number 71160-24-2
InChI Identifier InChI=1/C20H32O4/c1-2-3-4-5-6-9-13-18(21)14-10-7-8-11-15-19(22)16-12-17-20(23)24/h6-11,14-15,18-19,21-22H,2-5,12-13,16-17H2,1H3,(H,23,24)/b8-7+,9-6-,14-10+,15-11-/t18-,19-/m1/s1
Synthesis Reference Han, Chao Qi; DiTullio, Dennis; Wang, Yi Fong; Sih, Charles J. A chemoenzymatic synthesis of leukotriene B4. Journal of Organic Chemistry (1986), 51(8), 1253-8.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0152 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5.46 [Predicted by ALOGPS]; 0.7 [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
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Neutrophil
Platelet
Skin
Concentrations (Normal)
Biofluid Blood
Value 0.000296 +/- 0.000292 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]
  • Psychogios N, Hau DD, Peng J, Guo AC, Mandal R, Bouatra S, Sinelnikov I, Krishnamurthy R, Eisner R, Gautam B, Young N, Xia J, Knox C, Dong E, Huang P, Hollander Z, Pedersen TL, Smith SR, Bamforth F, Greiner R, McManus B, Newman JW, Goodfriend T, Wishart DS: The human serum metabolome. PLoS One. 2011 Feb 16;6(2):e16957. [PubMed Link Image]
Biofluid Blood
Value 3.7E-5 +/- 7E-6 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]
Biofluid CSF
Value 0.00011 +/- 0.00006 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 CSF
Value 0.000115 +/- 5.710e-05 uM
Age N/A
Sex N/A
Patient information Normal
Comments Not Available
References
  • Mayatepek E, Meissner T, Grobe H: Acute metabolic crisis with extreme deficiency of glutathione in combination with decreased levels of leukotriene C4 in a patient with glutathione synthetase deficiency. J Inherit Metab Dis. 2004;27(2):297-9. [PubMed Link Image]
Biofluid CSF
Value 0.00363 +/- 0.000480 uM
Age Children:1-13 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Matsuo M, Hamasaki Y, Masuyama T, Ohta M, Miyazaki S: Leukotriene B4 and C4 in cerebrospinal fluid from children with meningitis and febrile seizures. Pediatr Neurol. 1996 Feb;14(2):121-4. [PubMed Link Image]
Biofluid Urine
Value 0 - 0.000005 umol/mmol creatinine
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 0.00003 +/- 0.000014 umol/mmol creatinine
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]
Concentrations (Abnormal)
Biofluid Blood
Value 0.00015 +/- 0.00005 uM
Age Infant:0-1 yr old
Sex Both
Condition Cardiopulmonary bypass
Comments Samples were treated using modified ultrafiltration
References
  • Pearl JM, Manning PB, McNamara JL, Saucier MM, Thomas DW: Effect of modified ultrafiltration on plasma thromboxane B2, leukotriene B4, and endothelin-1 in infants undergoing cardiopulmonary bypass. Ann Thorac Surg. 1999 Oct;68(4):1369-75. [PubMed Link Image]
Biofluid Blood
Value 0.00016 +/- 0.00006 uM
Age Infant:0-1 yr old
Sex Both
Condition Cardiopulmonary bypass
Comments Samples were treated without modified ultrafiltration
References
  • Pearl JM, Manning PB, McNamara JL, Saucier MM, Thomas DW: Effect of modified ultrafiltration on plasma thromboxane B2, leukotriene B4, and endothelin-1 in infants undergoing cardiopulmonary bypass. Ann Thorac Surg. 1999 Oct;68(4):1369-75. [PubMed Link Image]
Biofluid CSF
Value 0.00014 +/- 0.00002 uM
Age Children:1-13 yrs old
Sex Both
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]
Biofluid CSF
Value 0.00477 +/- 0.000813 uM
Age Children:1-13 yrs old
Sex N/A
Comments Not Available
References
  • Matsuo M, Hamasaki Y, Masuyama T, Ohta M, Miyazaki S: Leukotriene B4 and C4 in cerebrospinal fluid from children with meningitis and febrile seizures. Pediatr Neurol. 1996 Feb;14(2):121-4. [PubMed Link Image]
Biofluid CSF
Value 0.000177 uM
Age Adult:>18 yrs old
Sex Male
Comments Not Available
References
  • Mayatepek E, Meissner T, Grobe H: Acute metabolic crisis with extreme deficiency of glutathione in combination with decreased levels of leukotriene C4 in a patient with glutathione synthetase deficiency. J Inherit Metab Dis. 2004;27(2):297-9. [PubMed Link Image]
Biofluid CSF
Value <0.000149 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value <0.000149 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value <0.000595 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Biofluid CSF
Value <0.000297 uM
Age N/A
Sex N/A
Comments Not Available
References
  • Westcott JY, Murphy RC, Stenmark K: Eicosanoids in human ventricular cerebrospinal fluid following severe brain injury. Prostaglandins. 1987 Dec;34(6):877-87. [PubMed Link Image]
Associated Disorders
Condition References
Cardiopulmonary bypass
  • Pearl JM, Manning PB, McNamara JL, Saucier MM, Thomas DW: Effect of modified ultrafiltration on plasma thromboxane B2, leukotriene B4, and endothelin-1 in infants undergoing cardiopulmonary bypass. Ann Thorac Surg. 1999 Oct;68(4):1369-75. [PubMed Link Image]
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. Emingil G, Coker I, Atilla G, Huseyinov A: Levels of leukotriene B4 and platelet activating factor in gingival crevicular fluid in renal transplant patients receiving cyclosporine A. J Periodontol. 2000 Jan;71(1):50-7. [PubMed Link Image]
  2. Ahmadzadeh N, Shingu M, Nobunaga M, Tawara T: Relationship between leukotriene B4 and immunological parameters in rheumatoid synovial fluids. Inflammation. 1991 Dec;15(6):497-503. [PubMed Link Image]
  3. Lambiase A, Bonini S, Rasi G, Coassin M, Bruscolini A, Bonini S: Montelukast, a leukotriene receptor antagonist, in vernal keratoconjunctivitis associated with asthma. Arch Ophthalmol. 2003 May;121(5):615-20. [PubMed Link Image]
  4. Nathan H, Naveh N, Meyer E: Levels of prostaglandin E2 and leukotriene B4 in tears of vernal conjunctivitis patients during a therapeutic trial with indomethacin. Doc Ophthalmol. 1994;85(3):247-57. [PubMed Link Image]
  5. Crocker I, Lawson N, Daniels I, Baker P, Fletcher J: Significance of fatty acids in pregnancy-induced immunosuppression. Clin Diagn Lab Immunol. 1999 Jul;6(4):587-93. [PubMed Link Image]
  6. Yanagisawa Y, Nagai T: [The relationship between serum leukotriene B4 and smoking] Nippon Eiseigaku Zasshi. 1993 Aug;48(3):698-706. [PubMed Link Image]
  7. Iversen L, Fogh K, Ziboh VA, Kristensen P, Schmedes A, Kragballe K: Leukotriene B4 formation during human neutrophil keratinocyte interactions: evidence for transformation of leukotriene A4 by putative keratinocyte leukotriene A4 hydrolase. J Invest Dermatol. 1993 Mar;100(3):293-8. [PubMed Link Image]
  8. Mancuso P, Nana-Sinkam P, Peters-Golden M: Leukotriene B4 augments neutrophil phagocytosis of Klebsiella pneumoniae. Infect Immun. 2001 Apr;69(4):2011-6. [PubMed Link Image]
  9. Mozalevskii AF, Travianko TD, Iakovlev AA, Smirnova EA, Novikova NP, Sapa IIu: [Content of arachidonic acid metabolites in blood and saliva of children with bronchial asthma] Ukr Biokhim Zh. 1997 Sep-Dec;69(5-6):162-8. [PubMed Link Image]
  10. Shindo K, Koide K, Fukumura M: Enhancement of leukotriene B4 release in stimulated asthmatic neutrophils by platelet activating factor. Thorax. 1997 Dec;52(12):1024-9. [PubMed Link Image]
  11. Sieunarine K, Lawrence-Brown MM, Goodman MA, Prendergast FJ, Rocchetta S: Plasma levels of the lipid mediators, leukotriene B4 and lyso platelet-activating factor, in intraoperative salvaged blood. Vox Sang. 1992;63(3):168-71. [PubMed Link Image]
  12. Blackburn WD Jr, Heck LW, Loose LD, Eskra JD, Carty TJ: Inhibition of 5-lipoxygenase product formation and polymorphonuclear cell degranulation by tenidap sodium in patients with rheumatoid arthritis. Arthritis Rheum. 1991 Feb;34(2):204-10. [PubMed Link Image]
  13. Soyombo O, Spur BW, Soh C, Lee TH: Structure/activity relationship of leukotriene B4 and its structural analogues in chemotactic, lysosomal-enzyme release and receptor-binding assays. Eur J Biochem. 1993 Nov 15;218(1):59-66. [PubMed Link Image]
  14. Garcia-Pastor P, Randazzo A, Gomez-Paloma L, Alcaraz MJ, Paya M: Effects of petrosaspongiolide M, a novel phospholipase A2 inhibitor, on acute and chronic inflammation. J Pharmacol Exp Ther. 1999 Apr;289(1):166-72. [PubMed Link Image]
  15. Nieminen MM, Moilanen EK, Koskinen MO, Karvonen JI, Tuomisto L, Metsa-Ketela TJ, Vapaatalo H: Inhaled budesonide fails to inhibit the PAF-induced increase in plasma leukotriene B4 in man. Br J Clin Pharmacol. 1992 Jun;33(6):645-52. [PubMed Link Image]
  16. Seyger MM, van Pelt JP, van den Born J, Latijnhouwers MA, de Jong EM: Epicutaneous application of leukotriene B4 induces patterns of tenascin and a heparan sulfate proteoglycan epitope that are typical for psoriatic lesions. Arch Dermatol Res. 1997 May;289(6):331-6. [PubMed Link Image]
  17. Berry KA, Borgeat P, Gosselin J, Flamand L, Murphy RC: Urinary metabolites of leukotriene B4 in the human subject. J Biol Chem. 2003 Jul 4;278(27):24449-60. Epub 2003 Apr 22. [PubMed Link Image]
  18. Pacheco Y, Hosni R, Chabannes B, Gormand F, Moliere P, Grosclaude M, Piperno D, Lagarde M, Perrin-Fayolle M: Leukotriene B4 level in stimulated blood neutrophils and alveolar macrophages from healthy and asthmatic subjects. Effect of beta-2 agonist therapy. Eur J Clin Invest. 1992 Nov;22(11):732-9. [PubMed Link Image]
  19. Bentancur AG, Naveh N, Lancri J, Selah BA, Livneh A: Urine leukotriene B4 in familial Mediterranean fever. Clin Exp Rheumatol. 2004 Jul-Aug;22(4 Suppl 34):S56-8. [PubMed Link Image]
  20. Fogh J, Poulsen LK, Bisgaard H: A specific assay for leukotriene B4 in human whole blood. J Pharmacol Toxicol Methods. 1992 Dec;28(4):185-90. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Leukotriene-B(4) omega-hydroxylase 1
  2. Leukotriene-B(4) omega-hydroxylase 2
  3. Leukotriene A-4 hydrolase
  4. Leukotriene B4 receptor 1
  5. Leukotriene B4 receptor 2
  6. Leukotriene B4 receptor
  7. cDNA FLJ53958, highly similar to Leukotriene B4 receptor 2
  8. G-protein coupled receptor
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
Enzyme 3 [top]
Enzyme 3 ID 6303
Enzyme 3 Name Leukotriene A-4 hydrolase
Enzyme 3 Synonyms
  1. LTA-4 hydrolase
  2. Leukotriene A(4) hydrolase
Enzyme 3 Gene Name LTA4H
Enzyme 3 Protein Sequence >Leukotriene A-4 hydrolase
MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDL
TIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLT
PEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETP
DPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETES
MLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISH
SWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGET
HPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSI
TTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAK
EDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWL
RLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVT
AMLVGKDLKVD
Enzyme 3 Number of Residues 611
Enzyme 3 Molecular Weight 69284.6
Enzyme 3 Theoretical pI 6.10
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ether hydrolase activity
  • hydrolase activity
  • hydrolase activity, acting on ether bonds
  • ion binding
  • leukotriene-A4 hydrolase activity
  • metal ion binding
  • metallopeptidase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • transition metal ion binding
  • zinc ion binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid metabolic process
  • icosanoid metabolic process
  • leukotriene biosynthetic process
  • leukotriene metabolic process
  • macromolecule metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
  • protein metabolic process
  • proteolysis
  • unsaturated fatty acid metabolic process
Component
Enzyme 3 General Function Involved in binding
Enzyme 3 Specific Function Hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4). The enzyme also has some peptidase activity
Enzyme 3 Pathways
Enzyme 3 Reactions
  • (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate [RN:R03057]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P09960 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name LKHA4_HUMAN Link Image
Enzyme 3 PDB ID 1HS6 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1836 bp
ATGCCCGAGATAGTGGATACCTGTTCGTTGGCCTCTCCGGCTTCCGTCTGCCGGACCAAG
CACCTGCACCTGCGCTGCAGCGTCGACTTTACTCGCCGGACGCTGACCGGGACTGCTGCT
CTCACGGTCCAGTCTCAGGAGGACAATCTGCGCAGCCTGGTTTTGGATACAAAGGACCTT
ACAATAGAAAAAGTAGTGATCAATGGACAAGAAGTCAAATATGCTCTTGGAGAAAGACAA
AGTTACAAGGGATCGCCAATGGAAATCTCTCTTCCTATCGCTTTGAGCAAAAATCAAGAA
ATTGTTATAGAAATTTCTTTTGAGACCTCTCCAAAATCTTCTGCTCTCCAGTGGCTCACT
CCTGAACAGACTTCTGGGAAGGAACACCCATATCTCTTTAGTCAGTGCCAGGCCATCCAC
TGCAGAGCAATCCTTCCTTGTCAGGACACTCCTTCTGTGAAATTAACCTATACTGCAGAG
GTGTCTGTCCCTAAAGAACTGGTGGCACTTATGAGTGCTATTCGTGATGGAGAAACACCT
GACCCAGAAGACCCAAGCAGGAAAATATACAAATTCATCCAAAAAGTTCCAATACCCTGC
TACCTGATTGCTTTAGTTGTTGGAGCTTTAGAAAGCAGGCAAATTGGCCCAAGAACTTTG
GTGTGGTCTGAGAAAGAGCAGGTGGAAAAGTCTGCTTATGAGTTTTCTGAGACTGAATCT
ATGCTTAAAATAGCAGAAGATCTGGGAGGACCGTATGTATGGGGACAGTATGACCTATTG
GTCCTGCCACCATCCTTCCCTTATGGTGGCATGGAGAATCCTTGCCTTACTTTTGTAACT
CCTACTCTACTGGCAGGCGACAAGTCACTCTCCAATGTCATTGCACATGAAATATCTCAT
AGCTGGACAGGGAATCTAGTGACCAACAAAACTTGGGATCACTTTTGGTTAAATGAGGGA
CATACTGTGTACTTGGAACGCCACATTTGCGGACGATTGTTTGGTGAAAAGTTCAGACAT
TTTAATGCTCTGGGAGGATGGGGAGAACTACAGAATTCGGTAAAGACATTTGGGGAGACA
CATCCTTTCACCAAACTTGTGGTTGATCTGACAGATATAGACCCTGATGTAGCTTATTCT
TCAGTTCCCTATGAGAAGGGCTTTGCTTTACTTTTTTACCTTGAACAACTGCTTGGAGGA
CCAGAGATTTTCCTAGGATTCTTAAAAGCTTATGTTGAGAAGTTTTCCTATAAGAGCATA
ACTACTGATGACTGGAAGGATTTCCTGTATTCCTATTTTAAAGATAAGGTTGATGTTCTC
AATCAAGTTGATTGGAATGCCTGGCTCTACTCTCCTGGACTGCCTCCCATAAAGCCCAAT
TATGATATGACTCTGACAAATGCTTGTATTGCCTTAAGTCAAAGATGGATTACTGCCAAA
GAAGATGATTTAAATTCATTCAATGCCACAGACCTGAAGGATCTCTCTTCTCATCAATTG
AATGAGTTTTTAGCACAGACGCTCCAGAGGGCACCTCTTCCATTGGGGCACATAAAGCGA
ATGCAAGAGGTGTACAACTTCAATGCCATTAACAATTCTGAAATACGATTCAGATGGCTG
CGGCTCTGCATTCAATCCAAGTGGGAGGACGCAATTCCTTTGGCGCTAAAGATGGCAACT
GAACAAGGAAGAATGAAGTTTACCCGGCCCTTATTCAAGGATCTTGCTGCCTTTGACAAA
TCCCATGATCAAGCTGTCCGAACCTACCAAGAGCACAAAGCAAGCATGCATCCCGTGACT
GCAATGCTGGTGGGGAAAGACTTAAAAGTGGATTAA
Enzyme 3 GenBank Gene ID J03459 Link Image
Enzyme 3 GeneCard ID LTA4H Link Image
Enzyme 3 GenAtlas ID LTA4H Link Image
Enzyme 3 HGNC ID HGNC:6710 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 12q22
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Minami M, Ohno S, Kawasaki H, Radmark O, Samuelsson B, Jornvall H, Shimizu T, Seyama Y, Suzuki K: Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase. Complete primary structure of an enzyme involved in eicosanoid synthesis. J Biol Chem. 1987 Oct 15;262(29):13873-6. [PubMed Link Image]
  2. Funk CD, Radmark O, Fu JY, Matsumoto T, Jornvall H, Shimizu T, Samuelsson B: Molecular cloning and amino acid sequence of leukotriene A4 hydrolase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6677-81. [PubMed Link Image]
  3. Mancini JA, Evans JF: Cloning and characterization of the human leukotriene A4 hydrolase gene. Eur J Biochem. 1995 Jul 1;231(1):65-71. [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. Odlander B, Claesson HE, Bergman T, Radmark O, Jornvall H, Haeggstrom JZ: Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji: indications of catalytically divergent forms of the enzyme. Arch Biochem Biophys. 1991 May 15;287(1):167-74. [PubMed Link Image]
  6. Radmark O, Shimizu T, Jornvall H, Samuelsson B: Leukotriene A4 hydrolase in human leukocytes. Purification and properties. J Biol Chem. 1984 Oct 25;259(20):12339-45. [PubMed Link Image]
  7. Jendraschak E, Kaminski WE, Kiefl R, von Schacky C: The human leukotriene A4 hydrolase gene is expressed in two alternatively spliced mRNA forms. Biochem J. 1996 Mar 15;314 ( Pt 3):733-7. [PubMed Link Image]
  8. Toh H, Minami M, Shimizu T: Molecular evolution and zinc ion binding motif of leukotriene A4 hydrolase. Biochem Biophys Res Commun. 1990 Aug 31;171(1):216-21. [PubMed Link Image]
  9. Haeggstrom JZ, Wetterholm A, Shapiro R, Vallee BL, Samuelsson B: Leukotriene A4 hydrolase: a zinc metalloenzyme. Biochem Biophys Res Commun. 1990 Nov 15;172(3):965-70. [PubMed Link Image]
  10. Medina JF, Wetterholm A, Radmark O, Shapiro R, Haeggstrom JZ, Vallee BL, Samuelsson B: Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7620-4. [PubMed Link Image]
  11. Minami M, Bito H, Ohishi N, Tsuge H, Miyano M, Mori M, Wada H, Mutoh H, Shimada S, Izumi T, et al.: Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of leukotriene A4 hydrolase and aminopeptidase activities by site-directed mutagenesis at Glu-297. FEBS Lett. 1992 Sep 14;309(3):353-7. [PubMed Link Image]
  12. Wetterholm A, Medina JF, Radmark O, Shapiro R, Haeggstrom JZ, Vallee BL, Samuelsson B: Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9141-5. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  14. Thunnissen MM, Nordlund P, Haeggstrom JZ: Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol. 2001 Feb;8(2):131-5. [PubMed Link Image]
  15. Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ: Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7211
Enzyme 4 Name Leukotriene B4 receptor 1
Enzyme 4 Synonyms
  1. LTB4-R 1
  2. LTB4-R1
  3. Chemoattractant receptor-like 1
  4. G-protein coupled receptor 16
  5. P2Y purinoceptor 7
  6. P2Y7
Enzyme 4 Gene Name LTB4R
Enzyme 4 Protein Sequence >Leukotriene B4 receptor 1
MNTTSSAAPPSLGVEFISLLAIILLSVALAVGLPGNSFVVWSILKRMQKRSVTALMVLNL
ALADLAVLLTAPFFLHFLAQGTWSFGLAGCRLCHYVCGVSMYASVLLITAMSLDRSLAVA
RPFVSQKLRTKAMARRVLAGIWVLSFLLATPVLAYRTVVPWKTNMSLCFPRYPSEGHRAF
HLIFEAVTGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILTFAAFWLPYHVV
NLAEAGRALAGQAAGLGLVGKRLSLARNVLIALAFLSSSVNPVLYACAGGGLLRSAGVGF
VAKLLEGTGSEASSTRRGGSLGQTARSGPAALEPGPSESLTASSPLKLNELN
Enzyme 4 Number of Residues 352
Enzyme 4 Molecular Weight 37556.9
Enzyme 4 Theoretical pI 11.63
Enzyme 4 GO Classification
Function
  • G-protein coupled receptor activity
  • leukotriene receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 4 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 4 Specific Function Receptor for extracellular ATP > UTP and ADP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. May be the cardiac P2Y receptor involved in the regulation of cardiac muscle contraction through modulation of L-type calcium currents. Is a receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 20-42 55-75 92-113 139-159 179-199 222-242 269-289
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 9229837 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q15722 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name LT4R1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1059 bp
ATGAACACTACATCTTCTGCAGCACCCCCCTCACTAGGTGTAGAGTTCATCTCTCTGCTG
GCTATCATCCTGCTGTCAGTGGCGCTGGCTGTGGGGCTTCCCGGCAACAGCTTTGTGGTG
TGGAGTATCCTGAAAAGGATGCAGAAGCGCTCTGTCACTGCCCTGATGGTGCTGAACCTG
GCCCTGGCCGACCTGGCCGTATTGCTCACTGCTCCCTTTTTCCTTCACTTCCTGGCCCAA
GGCACCTGGAGTTTTGGACTGGCTGGTTGCCGCCTGTGTCACTATGTCTGCGGAGTCAGC
ATGTACGCCAGCGTCCTGCTTATCACGGCCATGAGTCTAGACCGCTCACTGGCGGTGGCC
CGCCCCTTTGTGTCCCAGAAGCTACGCACCAAGGCGATGGCCCGGCGGGTGCTGGCAGGC
ATCTGGGTGTTGTCCTTTCTGCTGGCCACACCCGTCCTCGCGTACCGCACAGTAGTGCCC
TGGAAAACGAACATGAGCCTGTGCTTCCCGCGGTACCCCAGCGAAGGGCACCGGGCCTTC
CATCTAATCTTCGAGGCTGTCACGGGCTTCCTGCTGCCCTTCCTGGCTGTGGTGGCCAGC
TACTCGGACATAGGGCGTCGGCTACAGGCCCGGCGCTTCCGCCGCAGCCGCCGCACCGGC
CGCCTGGTGGTGCTCATCATCCTGACCTTCGCCGCCTTCTGGCTGCCCTACCACGTGGTG
AACCTGGCTGAGGCGGGCCGCGCGCTGGCCGGCCAGGCCGCCGGGTTAGGGCTCGTGGGG
AAGCGGCTGAGCCTGGCCCGCAACGTGCTCATCGCACTCGCCTTCCTGAGCAGCAGCGTG
AACCCCGTGCTGTACGCGTGCGCCGGCGGCGGCCTGCTGCGCTCGGCGGGCGTGGGCTTC
GTCGCCAAGCTGCTGGAGGGCACGGGCTCCGAGGCGTCCAGCACGCGCCGCGGGGGCAGC
CTGGGCCAGACCGCTAGGAGCGGCCCCGCCGCTCTGGAGCCCGGCCCTTCCGAGAGCCTC
ACTGCCTCCAGCCCTCTCAAGTTAAACGAACTGAACTAG
Enzyme 4 GenBank Gene ID AB008193 Link Image
Enzyme 4 GeneCard ID LTB4R Link Image
Enzyme 4 GenAtlas ID LTB4R Link Image
Enzyme 4 HGNC ID HGNC:6713 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 14q11.2-q12
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Akbar GK, Dasari VR, Webb TE, Ayyanathan K, Pillarisetti K, Sandhu AK, Athwal RS, Daniel JL, Ashby B, Barnard EA, Kunapuli SP: Molecular cloning of a novel P2 purinoceptor from human erythroleukemia cells. J Biol Chem. 1996 Aug 2;271(31):18363-7. [PubMed Link Image]
  2. Raport CJ, Schweickart VL, Chantry D, Eddy RL Jr, Shows TB, Godiska R, Gray PW: New members of the chemokine receptor gene family. J Leukoc Biol. 1996 Jan;59(1):18-23. [PubMed Link Image]
  3. Yokomizo T, Izumi T, Chang K, Takuwa Y, Shimizu T: A G-protein-coupled receptor for leukotriene B4 that mediates chemotaxis. Nature. 1997 Jun 5;387(6633):620-4. [PubMed Link Image]
  4. Owman C, Nilsson C, Lolait SJ: Cloning of cDNA encoding a putative chemoattractant receptor. Genomics. 1996 Oct 15;37(2):187-94. [PubMed Link Image]
  5. Kato K, Yokomizo T, Izumi T, Shimizu T: Cell-specific transcriptional regulation of human leukotriene B(4) receptor gene. J Exp Med. 2000 Aug 7;192(3):413-20. [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. Gaudreau R, Le Gouill C, Venne MH, Stankova J, Rola-Pleszczynski M: Threonine 308 within a putative casein kinase 2 site of the cytoplasmic tail of leukotriene B(4) receptor (BLT1) is crucial for ligand-induced, G-protein-coupled receptor-specific kinase 6-mediated desensitization. J Biol Chem. 2002 Aug 30;277(35):31567-76. Epub 2002 Jun 20. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13496
Enzyme 5 Name Leukotriene B4 receptor 2
Enzyme 5 Synonyms
  1. LTB4-R 2
  2. LTB4-R2
  3. LTB4 receptor JULF2
  4. Leukotriene B4 receptor BLT2
  5. Seven transmembrane receptor BLTR2
Enzyme 5 Gene Name LTB4R2
Enzyme 5 Protein Sequence >Leukotriene B4 receptor 2
MAPSHRASQVGFCPTPERPLWRLPPTCRPRRMSVCYRPPGNETLLSWKTSRATGTAFLLL
AALLGLPGNGFVVWSLAGWRPARGRPLAATLVLHLALADGAVLLLTPLFVAFLTRQAWPL
GQAGCKAVYYVCALSMYASVLLTGLLSLQRCLAVTRPFLAPRLRSPALARRLLLAVWLAA
LLLAVPAAVYRHLWRDRVCQLCHPSPVHAAAHLSLETLTAFVLPFGLMLGCYSVTLARLR
GARWGSGRHGARVGRLVSAIVLAFGLLWAPYHAVNLLQAVAALAPPEGALAKLGGAGQAA
RAGTTALAFFSSSVNPVLYVFTAGDLLPRAGPRFLTRLFEGSGEARGGGRSREGTMELRT
TPQLKVVGQGRGNGDPGGGMEKDGPEWDL
Enzyme 5 Number of Residues 389
Enzyme 5 Molecular Weight 41524.3
Enzyme 5 Theoretical pI 11.49
Enzyme 5 GO Classification
Function
  • G-protein coupled receptor activity
  • leukotriene receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 5 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 5 Specific Function Low-affinity receptor for leukotrienes including leukotriene B4. Mediates chemotaxis of granulocytes and macrophages. The response is mediated via G-proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinities for the leukotrienes is LTB4 > 12-epi-LTB4 > LTB5 > LTB3
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 56-76 92-112 128-148 173-193 217-237 257-277 307-327
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID Q9NPC1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name LT4R2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1170 bp
ATGGCACCTTCTCATCGGGCATCACAGGTGGGGTTTTGCCCCACCCCTGAACGCCCTCTG
TGGCGCCTTCCACCCACCTGTAGGCCCAGAAGGATGTCGGTCTGCTACCGTCCCCCAGGG
AACGAGACACTGCTGAGCTGGAAGACTTCGCGGGCCACAGGCACAGCCTTCCTGCTGCTG
GCGGCGCTGCTGGGGCTGCCTGGCAACGGCTTCGTGGTGTGGAGCTTGGCGGGCTGGCGG
CCTGCACGGGGGCGACCGCTGGCGGCCACGCTTGTGCTGCACCTGGCGCTGGCCGACGGC
GCGGTGCTGCTGCTCACGCCGCTCTTTGTGGCCTTCCTGACCCGGCAGGCCTGGCCGCTG
GGCCAGGCGGGCTGCAAGGCGGTGTACTACGTGTGCGCGCTCAGCATGTACGCCAGCGTG
CTGCTCACCGGCCTGCTCAGCCTGCAGCGCTGCCTCGCAGTCACCCGCCCCTTCCTGGCG
CCTCGGCTGCGCAGCCCGGCCCTGGCCCGCCGCCTGCTGCTGGCGGTCTGGCTGGCCGCC
CTGTTGCTCGCCGTCCCGGCCGCCGTCTACCGCCACCTGTGGAGGGACCGCGTATGCCAG
CTGTGCCACCCGTCGCCGGTCCACGCCGCCGCCCACCTGAGCCTGGAGACTCTGACCGCT
TTCGTGCTTCCTTTCGGGCTGATGCTCGGCTGCTACAGCGTGACGCTGGCACGGCTGCGG
GGCGCCCGCTGGGGCTCCGGGCGGCACGGGGCGCGGGTGGGCCGGCTGGTGAGCGCCATC
GTGCTTGCCTTCGGCTTGCTCTGGGCCCCCTACCACGCAGTCAACCTTCTGCAGGCGGTC
GCAGCGCTGGCTCCACCGGAAGGGGCCTTGGCGAAGCTGGGCGGAGCCGGCCAGGCGGCG
CGAGCGGGAACTACGGCCTTGGCCTTCTTCAGTTCTAGCGTCAACCCGGTGCTCTACGTC
TTCACCGCTGGAGATCTGCTGCCCCGGGCAGGTCCCCGTTTCCTCACGCGGCTCTTCGAA
GGCTCTGGGGAGGCCCGAGGGGGCGGCCGCTCTAGGGAAGGGACCATGGAGCTCCGAACT
ACCCCTCAGCTGAAAGTGGTGGGGCAGGGCCGCGGCAATGGAGACCCGGGGGGTGGGATG
GAGAAGGACGGTCCGGAATGGGACCTTTGA
Enzyme 5 GenBank Gene ID AF277230 Link Image
Enzyme 5 GeneCard ID LTB4R2 Link Image
Enzyme 5 GenAtlas ID LTB4R2 Link Image
Enzyme 5 HGNC ID HGNC:19260 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 14q11.2-q12
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Tryselius Y, Nilsson NE, Kotarsky K, Olde B, Owman C: Cloning and characterization of cDNA encoding a novel human leukotriene B(4) receptor. Biochem Biophys Res Commun. 2000 Aug 2;274(2):377-82. [PubMed Link Image]
  2. Yokomizo T, Kato K, Terawaki K, Izumi T, Shimizu T: A second leukotriene B(4) receptor, BLT2. A new therapeutic target in inflammation and immunological disorders. J Exp Med. 2000 Aug 7;192(3):421-32. [PubMed Link Image]
  3. Wang S, Gustafson E, Pang L, Qiao X, Behan J, Maguire M, Bayne M, Laz T: A novel hepatointestinal leukotriene B4 receptor. Cloning and functional characterization. J Biol Chem. 2000 Dec 29;275(52):40686-94. [PubMed Link Image]
  4. Kamohara M, Takasaki J, Matsumoto M, Saito T, Ohishi T, Ishii H, Furuichi K: Molecular cloning and characterization of another leukotriene B4 receptor. J Biol Chem. 2000 Sep 1;275(35):27000-4. [PubMed Link Image]
  5. Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 17162
Enzyme 6 Name Leukotriene B4 receptor
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name Not Available
Enzyme 6 Protein Sequence >Leukotriene B4 receptor
MNTTSSAAPPSLGVEFISLLAIILLSVALAVGLPGNSFVVWSILKRMQKRSVTALMVLNL
ALADLAVLLTAPFFLHFLAQGTWSFGLAGCRLCHYVCGVSMYASVLLITAMSLDRSLAVA
RPFVSQKLRTKAMARRVLAGIWVLSFLLATPVLAYRTVVPWKTNMSLCFPRYPSEGHRAF
HLIFEAVTGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILTFAAFWLPYHVV
NLAEAGRALAGQAAGLGLVGKRLSLARNVLIALAFLSSSVNPVLYACAGGGLLRSAGVGF
VAKLLEGTGSEASSTRRGGSLGQTARSGPAALEPGPSESLTASSPFKLNELN
Enzyme 6 Number of Residues 352
Enzyme 6 Molecular Weight 37592
Enzyme 6 Theoretical pI 11.63
Enzyme 6 GO Classification
Function
  • G-protein coupled receptor activity
  • leukotriene receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID Q53XV5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q53XV5_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID BT007267 Link Image
Enzyme 6 GeneCard ID Q53XV5 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID HGNC:6713 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs Not Available
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 17163
Enzyme 7 Name cDNA FLJ53958, highly similar to Leukotriene B4 receptor 2
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name Not Available
Enzyme 7 Protein Sequence >cDNA FLJ53958, highly similar to Leukotriene B4 receptor 2
MSVCYRPPGNETLLSWKTSRATGTAFLLLAALLGLPGNGFVVWSLAGWRPARGRPLAATL
VLHLALADGAVLLLTPLFVAFLTRQAWPLGQAGCKAVYYVCALSMYASVLLTGLLSLQRC
LAVTRPFLAPRLRSPALARRLLLAVWLAALLLAVPAAVYRHLWRDRVCQLCHPSPVHAAA
HLSLETLTAFVLPFGLMLGCYSVTLARLRGARWGSGRHGARVGRLVSAIVLAFGLLWAPY
HAVNLLQAVAALAPPEGALAKLGGAGQAARAGTTALAFFSSSVDPVLYVFTAGDLLPRAG
PRFLTRLFEGSGEARGGGRSREGTMELRTTPQLKVVGQGRGNGDPGGGMEKDGPEWDL
Enzyme 7 Number of Residues 358
Enzyme 7 Molecular Weight 37942.2
Enzyme 7 Theoretical pI 10.99
Enzyme 7 GO Classification
Function
  • G-protein coupled receptor activity
  • leukotriene receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 7 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 194385354 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID B4E292 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B4E292_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1077 bp
ATGTCGGTCTGCTACCGTCCCCCAGGGAACGAGACACTGCTGAGCTGGAAGACTTCGCGG
GCCACAGGCACAGCCTTCCTGCTGCTGGCGGCGCTGCTGGGGCTGCCTGGCAACGGCTTC
GTGGTGTGGAGCTTGGCGGGCTGGCGGCCTGCACGGGGGCGACCGCTGGCGGCCACGCTT
GTGCTGCACCTGGCGCTGGCCGACGGCGCGGTGCTGCTGCTCACGCCGCTCTTTGTGGCC
TTCCTGACCCGGCAGGCCTGGCCGCTGGGCCAGGCGGGCTGCAAGGCGGTGTACTACGTG
TGCGCGCTCAGCATGTACGCCAGCGTGCTGCTCACCGGCCTGCTCAGCCTGCAGCGCTGC
CTCGCAGTCACCCGCCCCTTCCTGGCGCCTCGGCTGCGCAGCCCGGCCCTGGCCCGCCGC
CTGCTGCTGGCGGTCTGGCTGGCCGCCCTGTTGCTCGCCGTCCCGGCCGCCGTCTACCGC
CACCTGTGGAGGGACCGCGTATGCCAGCTGTGCCACCCGTCGCCGGTCCACGCCGCCGCC
CACCTGAGCCTGGAGACTCTGACCGCTTTCGTGCTTCCTTTCGGGCTGATGCTCGGCTGC
TACAGCGTGACGCTGGCACGGCTGCGGGGCGCCCGCTGGGGCTCCGGGCGGCACGGGGCG
CGGGTGGGCCGGCTGGTGAGCGCCATCGTGCTTGCCTTCGGCTTGCTCTGGGCCCCCTAC
CACGCAGTCAACCTTCTGCAGGCGGTCGCAGCGCTGGCTCCACCGGAAGGGGCCTTGGCG
AAGCTGGGCGGAGCCGGCCAGGCGGCGCGAGCGGGAACTACGGCCTTGGCCTTCTTCAGT
TCTAGCGTCGACCCGGTGCTCTACGTCTTCACCGCTGGAGATCTGCTGCCCCGGGCAGGT
CCCCGTTTCCTCACGCGGCTCTTCGAAGGCTCTGGGGAGGCCCGAGGGGGCGGCCGCTCT
AGGGAAGGGACCATGGAGCTCCGAACTACCCCTCAGCTGAAAGTGGTGGGGCAGGGCCGC
GGCAATGGAGACCCGGGGGGTGGGATGGAGAAGGACGGTCCGGAATGGGACCTTTGA
Enzyme 7 GenBank Gene ID AK304169 Link Image
Enzyme 7 GeneCard ID Not Available
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID HGNC:19260 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs Not Available
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 17164
Enzyme 8 Name G-protein coupled receptor
Enzyme 8 Synonyms
  1. SubName: HCG2043009
Enzyme 8 Gene Name KPG_004
Enzyme 8 Protein Sequence >G-protein coupled receptor
MSVCYRPPGNETLLSWKTSRATGTAFLLLAALLGLPGNGFVVWSLAGWRPARGRPLAATL
VLHLALADGAVLLLTPLFVAFLTRQAWPLGQAGCKAVYYVCALSMYASVLLTGLLSLQRC
LAVTRPFLAPRLRSPALARRLLLAVWLAALLLAVPAAVYRHLWRDRVCQLCHPSPVHAAA
HLSLETLTAFVLPFGLMLGCYSVTLARLRGARWGSGRHGARVGRLVSAIVLAFGLLWAPY
HAVNLLQAVAALAPPEGALAKLGGAGQAARAGTTALAFFSSSVNPVLYVFTAGDLLPRAG
PRFLTRLFEGSGEARGGGRSREGTMELRTTPQLKVVGQGRGNGDPGGGMEKDGPEWDL
Enzyme 8 Number of Residues 358
Enzyme 8 Molecular Weight 37941.2
Enzyme 8 Theoretical pI 11.14
Enzyme 8 GO Classification
Function
  • G-protein coupled receptor activity
  • leukotriene receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 8 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 57157113 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q5KU28 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q5KU28_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1077 bp
ATGTCGGTCTGCTACCGTCCCCCAGGGAACGAGACACTGCTGAGCTGGAAGACTTCGCGG
GCCACAGGCACAGCCTTCCTGCTGCTGGCGGCGCTGCTGGGGCTGCCTGGCAACGGCTTC
GTGGTGTGGAGCTTGGCGGGCTGGCGGCCTGCACGGGGGCGACCGCTGGCGGCCACGCTT
GTGCTGCACCTGGCGCTGGCCGACGGCGCGGTGCTGCTGCTCACGCCGCTCTTTGTGGCC
TTCCTGACCCGGCAGGCCTGGCCGCTGGGCCAGGCGGGCTGCAAGGCGGTGTACTACGTG
TGCGCGCTCAGCATGTACGCCAGCGTGCTGCTCACCGGCCTGCTCAGCCTGCAGCGCTGC
CTCGCAGTCACCCGCCCCTTCCTGGCGCCTCGGCTGCGCAGCCCGGCCCTGGCCCGCCGC
CTGCTGCTGGCGGTCTGGCTGGCCGCCCTGTTGCTCGCCGTCCCGGCCGCCGTCTACCGC
CACCTGTGGAGGGACCGCGTATGCCAGCTGTGCCACCCGTCGCCGGTCCACGCCGCCGCC
CACCTGAGCCTGGAGACTCTGACCGCTTTCGTGCTTCCTTTCGGGCTGATGCTCGGCTGC
TACAGCGTGACGCTGGCACGGCTGCGGGGCGCCCGCTGGGGCTCCGGGCGGCACGGGGCG
CGGGTGGGCCGGCTGGTGAGCGCCATCGTGCTTGCCTTCGGCTTGCTCTGGGCCCCCTAC
CACGCAGTCAACCTTCTGCAGGCGGTCGCAGCGCTGGCTCCACCGGAAGGGGCCTTGGCG
AAGCTGGGCGGAGCCGGCCAGGCGGCGCGAGCGGGAACTACGGCCTTGGCCTTCTTCAGT
TCTAGCGTCAACCCGGTGCTCTACGTCTTCACCGCTGGAGATCTGCTGCCCCGGGCAGGT
CCCCGTTTCCTCACGCGGCTCTTCGAAGGCTCTGGGGAGGCCCGAGGGGGCGGCCGCTCT
AGGGAAGGGACCATGGAGCTCCGAACTACCCCTCAGCTGAAAGTGGTGGGGCAGGGCCGC
GGCAATGGAGACCCGGGGGGTGGGATGGAGAAGGACGGTCCGGAATGGGACCTTTGA
Enzyme 8 GenBank Gene ID AB032558 Link Image
Enzyme 8 GeneCard ID KPG_004 Link Image
Enzyme 8 GenAtlas ID KPG_004 Link Image
Enzyme 8 HGNC ID HGNC:19260 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available