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Human Metabolome Database Version 2.5

 

Showing metabocard for Leukotriene A4 (HMDB01337)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-28 13:37:08
Accession Number HMDB01337
Secondary Accession Numbers Not Available
Common Name Leukotriene A4
Description Leukotriene A4 (LTA4) is the first metabolite in the series of reactions leading to the synthesis of all leukotrienes. 5-Lipoxygenase (5-LO) catalyzes the two-step conversion of arachidonic acid to LTA4.The first step consists of the oxidation of arachidonic acid to the unstable intermediate 5-hydroperoxyeicosatetraenoic acid (5-HPETE), and the second step is the dehydration of 5-HPETE to form LTA4. Leukotriene A4, an unstable epoxide, is hydrolyzed to leukotriene B4 or conjugated with glutathione to yield leukotriene C4 and its metabolites, leukotriene D4 and leukotriene E4. The leukotrienes participate in host defense reactions and pathophysiological conditions such as immediate hypersensitivity and inflammation. Recent studies also suggest a neuroendocrine role for leukotriene C4 in luteinizing hormone secretion. (PMID: 10591081, 2820055) 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. LTA4
  2. 5S,6S-epoxy-7E,9E,11Z,14Z-eicosatetraenoic acid
  3. (7e,9e,11z,14z)-(5s,6s)-5,6-epoxyicosa-7,9,11,14-tetrenoioc acid
  4. 5S,6S-epoxy-7E,9E,11Z,14Z-eicosatetraenoate
  5. (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa- 7,9,11,14-tetraenoate
  6. (7E,9E,11Z,14Z)-(5S,6S)-5,6-Epoxyeicosa-7,9,11,14-tetraenoate
  7. (5S,6S,7E,9E,11Z,14Z)-5,6-Epoxyicosa-7,9,11,14-tetraenoate
  8. (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa- 7,9,11,14-tetraenoic acid
  9. (7E,9E,11Z,14Z)-(5S,6S)-5,6-Epoxyeicosa-7,9,11,14-tetraenoic acid
  10. (5S,6S,7E,9E,11Z,14Z)-5,6-Epoxyicosa-7,9,11,14-tetraenoic acid
Chemical IUPAC Name 4-[(2S,3S)-3-[(1E,3E,5Z,8Z)-tetradeca-1,3,5,8-tetraenyl]oxiran-2-yl]butanoic acid
Chemical Formula C20H30O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Leukotrienes
Family
  • Mammalian Metabolite
Species
  • dialkyl ether
  • carboxylic acid
  • alkene
  • heterocyclic compound
Biofunction
  • Component of Prostaglandin and leukotriene metabolism
Application
Source
  • Endogenous
Average Molecular Weight 318.450
Monoisotopic Molecular Weight 318.219482
Isomeric SMILES CCCCCC=C/CC=C/C=C/C=C/[C@@H]1O[C@H]1CCCC(O)=O
Canonical SMILES CCCCCC=CCC=CC=CC=CC1OC1CCCC(O)=O
KEGG Compound ID C00909 Link Image
BioCyc ID CPD-8892 Link Image
BiGG ID 36355 Link Image
Wikipedia Link Leukotriene A4 Link Image
NuGOwiki Link HMDB01337 Link Image
Metagene Link HMDB01337 Link Image
METLIN ID 3449 Link Image
PubChem Compound 5280383 Link Image
PubChem Substance 8143275 Link Image
ChEBI ID 15651 Link Image
CAS Registry Number 72059-45-1
InChI Identifier InChI=1/C20H30O3/c1-2-3-4-5-6-7-8-9-10-11-12-13-15-18-19(23-18)16-14-17-20(21)22/h6-7,9-13,15,18-19H,2-5,8,14,16-17H2,1H3,(H,21,22)/b7-6-,10-9-,12-11+,15-13+/t18-,19-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.24e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5 [Predicted by PubChem via XLOGP]; 6.04 [Predicted by ALOGPS] 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 Not Available
Tissue Location
Tissue References
Epidermis
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
General References
  1. Luscinskas FW, Nicolaou KC, Webber SE, Veale CA, Gimbrone MA Jr, Serhan CN: Ca2+ mobilization with leukotriene A4 and epoxytetraenes in human neutrophils. Biochem Pharmacol. 1990 Jan 15;39(2):355-65. [PubMed Link Image]
  2. 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]
  3. MacMillan DK, Hill E, Sala A, Sigal E, Shuman T, Henson PM, Murphy RC: Eosinophil 15-lipoxygenase is a leukotriene A4 synthase. J Biol Chem. 1994 Oct 28;269(43):26663-8. [PubMed Link Image]
  4. Iversen L, Ziboh VA, Shimizu T, Ohishi N, Radmark O, Wetterholm A, Kragballe K: Identification and subcellular localization of leukotriene A4-hydrolase activity in human epidermis. J Dermatol Sci. 1994 Jun;7(3):191-201. [PubMed Link Image]
  5. Nicholson DW, Klemba MW, Rasper DM, Metters KM, Zamboni RJ, Ford-Hutchinson AW: Purification of human leukotriene C4 synthase from dimethylsulfoxide-differentiated U937 cells. Eur J Biochem. 1992 Oct 15;209(2):725-34. [PubMed Link Image]
  6. Wikipedia Link Image
Metabolic Enzymes
  1. Leukotriene C4 synthase
  2. Arachidonate 5-lipoxygenase
  3. Leukotriene A-4 hydrolase
Enzyme 1 [top]
Enzyme 1 ID 6087
Enzyme 1 Name Leukotriene C4 synthase
Enzyme 1 Synonyms
  1. LTC4 synthase
  2. Leukotriene-C(4) synthase
Enzyme 1 Gene Name LTC4S
Enzyme 1 Protein Sequence >Leukotriene C4 synthase
MKDEVALLAAVTLLGVLLQAYFSLQVISARRAFRVSPPLTTGPPEFERVYRAQVNCSEYF
PLFLATLWVAGIFFHEGAAALCGLVYLFARLRYFQGYARSAQLRLAPLYASARALWLLVA
LAALGLLAHFLPAALRAALLGRLRTLLPWA
Enzyme 1 Number of Residues 150
Enzyme 1 Molecular Weight 16566.5
Enzyme 1 Theoretical pI 10.40
Enzyme 1 GO Classification
Function
  • enzyme activator activity
  • enzyme regulator activity
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid metabolic process
  • icosanoid metabolic process
  • leukotriene metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxoacid metabolic process
  • unsaturated fatty acid metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 1 General Function Involved in enzyme activator activity
Enzyme 1 Specific Function Catalyzes the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4
Enzyme 1 Pathways
Enzyme 1 Reactions
  • leukotriene C4 = leukotriene A4 + glutathione [RN:R03059]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 7-27 49-69 74-94 105-124
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q16873 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LTC4S_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >453 bp
ATGAAGGACGAGGTAGCTCTACTGGCTGCTGTCACCCTCCTGGGAGTCCTGCTGCAAGCC
TACTTCTCCCTGCAGGTGATCTCGGCGCGCAGGGCCTTCCGCGTGTCGCCGCCGCTCACC
ACCGGCCCACCCGAGTTCGAGCGCGTCTACCGAGCCCAGGTGAACTGCAGCGAGTACTTC
CCGCTGTTCCTCGCCACGCTCTGGGTCGCCGGCATCTTCTTTCATGAAGGGGCGGCGGCC
CTGTGCGGCCTGGTCTACCTGTTCGCGCGCCTCCGCTACTTCCAGGGCTACGCGCGCTCC
GCGCAGCTCAGGCTGGCACCGCTGTACGCGAGCGCGCGCGCCCTCTGGCTGCTGGTGGCG
CTGGCTGCGCTCGGCCTGCTCGCCCACTTCCTCCCGGCCGCGCTGCGCGCCGCGCTCCTC
GGACGGCTCCGGACGCTGCTGCCGTGGGCCTGA
Enzyme 1 GenBank Gene ID U09353 Link Image
Enzyme 1 GeneCard ID LTC4S Link Image
Enzyme 1 GenAtlas ID LTC4S Link Image
Enzyme 1 HGNC ID HGNC:6719 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5q35
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Lam BK, Penrose JF, Freeman GJ, Austen KF: Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7663-7. [PubMed Link Image]
  2. Welsch DJ, Creely DP, Hauser SD, Mathis KJ, Krivi GG, Isakson PC: Molecular cloning and expression of human leukotriene-C4 synthase. Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9745-9. [PubMed Link Image]
  3. Penrose JF, Spector J, Baldasaro M, Xu K, Boyce J, Arm JP, Austen KF, Lam BK: Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35. J Biol Chem. 1996 May 10;271(19):11356-61. [PubMed Link Image]
  4. Bigby TD, Hodulik CR, Arden KC, Fu L: Molecular cloning of the human leukotriene C4 synthase gene and assignment to chromosome 5q35. Mol Med. 1996 Sep;2(5):637-46. [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. Nicholson DW, Ali A, Vaillancourt JP, Calaycay JR, Mumford RA, Zamboni RJ, Ford-Hutchinson AW: Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):2015-9. [PubMed Link Image]
  7. Penrose JF, Spector J, Lam BK, Friend DS, Xu K, Jack RM, Austen KF: Purification of human lung leukotriene C4 synthase and preparation of a polyclonal antibody. Am J Respir Crit Care Med. 1995 Jul;152(1):283-9. [PubMed Link Image]
  8. Goppelt-Struebe M: Two step purification of human and murine leukotriene C4 synthase. Biochim Biophys Acta. 1995 May 17;1256(2):257-61. [PubMed Link Image]
  9. Mayatepek E, Flock B: Leukotriene C4-synthesis deficiency: a new inborn error of metabolism linked to a fatal developmental syndrome. Lancet. 1998 Nov 7;352(9139):1514-7. [PubMed Link Image]
  10. Mayatepek E, Zelezny R, Lehmann WD, Hammond JW, Hoffmann GF: Defects in the synthesis of cysteinyl leukotrienes: a new group of inborn errors of metabolism. J Inherit Metab Dis. 2000 Jun;23(4):404-8. [PubMed Link Image]
  11. Christmas P, Weber BM, McKee M, Brown D, Soberman RJ: Membrane localization and topology of leukotriene C4 synthase. J Biol Chem. 2002 Aug 9;277(32):28902-8. Epub 2002 May 21. [PubMed Link Image]
  12. Strid T, Svartz J, Franck N, Hallin E, Ingelsson B, Soderstrom M, Hammarstrom S: Distinct parts of leukotriene C(4) synthase interact with 5-lipoxygenase and 5-lipoxygenase activating protein. Biochem Biophys Res Commun. 2009 Apr 17;381(4):518-22. Epub 2009 Feb 20. [PubMed Link Image]
  13. Ago H, Kanaoka Y, Irikura D, Lam BK, Shimamura T, Austen KF, Miyano M: Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature. 2007 Aug 2;448(7153):609-12. Epub 2007 Jul 15. [PubMed Link Image]
  14. Martinez Molina D, Wetterholm A, Kohl A, McCarthy AA, Niegowski D, Ohlson E, Hammarberg T, Eshaghi S, Haeggstrom JZ, Nordlund P: Structural basis for synthesis of inflammatory mediators by human leukotriene C4 synthase. Nature. 2007 Aug 2;448(7153):613-6. Epub 2007 Jul 15. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6260
Enzyme 2 Name Arachidonate 5-lipoxygenase
Enzyme 2 Synonyms
  1. 5-LO
  2. 5-lipoxygenase
Enzyme 2 Gene Name ALOX5
Enzyme 2 Protein Sequence >Arachidonate 5-lipoxygenase
MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDE
ELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLA
RDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVL
NYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNG
CNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDP
CTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDF
HVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECG
LFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWE
AIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYL
TVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCW
HLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPY
YYLSPDRIPNSVAI
Enzyme 2 Number of Residues 674
Enzyme 2 Molecular Weight 77982.6
Enzyme 2 Theoretical pI 5.54
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • lipoxygenase activity
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • transition metal ion binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid metabolic process
  • icosanoid metabolic process
  • leukotriene metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
  • unsaturated fatty acid metabolic process
Component
Enzyme 2 General Function Involved in metal ion binding
Enzyme 2 Specific Function Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (1) arachidonate + O2 = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O (overall reaction) [RN:R08527]
  • (2) (1a) arachidonate + O2 = (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate [RN:R01595]
  • (3) (1b) (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O [RN:R03058]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
Enzyme 2 UniProtKB/Swiss-Prot ID P09917 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name LOX5_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2025 bp
ATGCCCTCCTACACGGTCACCGTGGCCACTGGCAGCCAGTGGTTCGCCGGCACTGACGAC
TACATCTACCTCAGCCTCGTGGGCTCGGCGGGCTGCAGCGAGAAGCACCTGCTGGACAAG
CCCTTCTACAACGACTTCGAGCGTGGCGCGGTGGATTCATACGACGTGACTGTGGACGAG
GAACTGGGCGAGATCCAGCTGGTCAGAATCGAGAAGCGCAAGTACTGGCTGAATGACGAC
TGGTACCTGAAGTACATCACGCTGAAGACGCCCCACGGGGACTACATCGAGTTCCCCTGC
TACCGCTGGATCACCGGCGATGTCGAGGTTGTCCTGAGGGATGGACGCGCAAAGTTGGCC
CGAGATGACCAAATTCACATTCTCAAGCAACACCGACGTAAAGAACTGGAAACACGGCAA
AAACAATATCGATGGATGGAGTGGAACCCTGGCTTCCCCTTGAGCATCGATGCCAAATGC
CACAAGGATTTACCCCGTGATATCCAGTTTGATAGTGAAAAAGGAGTGGACTTTGTTCTG
AATTACTCCAAAGCGATGGAGAACCTGTTCATCAACCGCTTCATGCACATGTTCCAGTCT
TCTTGGAATGACTTCGCCGACTTTGAGAAAATCTTTGTCAAGATCAGCAACACTATTTCT
GAGCGGGTCATGAATCACTGGCAGGAAGACCTGATGTTTGGCTACCAGTTCCTGAATGGC
TGCAACCCTGTGTTGATCCGGCGCTGCACAGAGCTGCCCGAGAAGCTCCCGGTGACCACG
GAGATGGTAGAGTGCAGCCTGGAGCGGCAGCTCAGCTTGGAGCAGGAGGTCCAGCAAGGG
AACATTTTCATCGTGGACTTTGAGCTGCTGGATGGCATCGATGCCAACAAAACAGACCCC
TGCACACTCCAGTTCCTGGCCGCTCCCATCTGCTTGCTGTATAAGAACCTGGCCAACAAG
ATTGTCCCCATTGCCATCCAGCTCAACCAAATCCCGGGAGATGAGAACCCTATTTTCCTC
CCTTCGGATGCAAAATACGACTGGCTTTTGGCCAAAATCTGGGTGCGTTCCAGTGACTTC
CACGTCCACCAGACCATCACCCACCTTCTGCGAACACATCTGGTGTCTGAGGTTTTTGGC
ATTGCAATGTACCGCCAGCTGCCTGCTGTGCACCCCATTTTCAAGCTGCTGGTGGCACAC
GTGAGATTCACCATTGCAATCAACACCAAGGCCCGTGAGCAGCTCATCTGCGAGTGTGGC
CTCTTTGACAAGGCCAACGCCACAGGGGGCGGTGGGCACGTGCAGATGGTGCAGAGGGCC
ATGAAGGACCTGACCTATGCCTCCCTGTGCTTTCCCGAGGCCATCAAGGCCCGGGGCATG
GAGAGCAAAGAAGACATCCCCTACTACTTCTACCGGGACGACGGGCTCCTGGTGTGGGAA
GCCATCAGGACGTTCACGGCCGAGGTGGTAGACATCTACTACGAGGGCGACCAGGTGGTG
GAGGAGGACCCGGAGCTGCAGGACTTCGTGAACGATGTCTACGTGTACGGCATGCGGGGC
CGCAAGTCCTCAGGCTTCCCCAAGTCGGTCAAGAGCCGGGAGCAGCTGTCGGAGTACCTG
ACCGTGGTGATCTTCACCGCCTCCGCCCAGCACGCCGCGGTCAACTTCGGCCAGTACGAC
TGGTGCTCCTGGATCCCCAATGCGCCCCCAACCATGCGAGCCCCGCCACCGACTGCCAAG
GGCGTGGTGACCATTGAGCAGATCGTGGACACGCTGCCCGACCGCGGCCGCTCCTGCTGG
CATCTGGGTGCAGTGTGGGCGCTGAGCCAGTTCCAGGAAAACGAGCTGTTCCTGGGCATG
TACCCAGAAGAGCATTTTATCGAGAAGCCTGTGAAGGAAGCCATGGCCCGATTCCGCAAG
AACCTCGAGGCCATTGTCAGCGTGATTGCTGAGCGCAACAAGAAGAAGCAGCTGCCATAT
TACTACTTGTCCCCAGACCGGATTCCGAACAGTGTGGCCATCTGA
Enzyme 2 GenBank Gene ID J03600 Link Image
Enzyme 2 GeneCard ID ALOX5 Link Image
Enzyme 2 GenAtlas ID ALOX5 Link Image
Enzyme 2 HGNC ID HGNC:435 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 10q11.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Dixon RA, Jones RE, Diehl RE, Bennett CD, Kargman S, Rouzer CA: Cloning of the cDNA for human 5-lipoxygenase. Proc Natl Acad Sci U S A. 1988 Jan;85(2):416-20. [PubMed Link Image]
  2. Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B: Molecular cloning and amino acid sequence of human 5-lipoxygenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):26-30. [PubMed Link Image]
  3. Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B: Molecular cloning and amino acid sequence of human 5-lipoxygenase. Adv Prostaglandin Thromboxane Leukot Res. 1989;19:466-9. [PubMed Link Image]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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. Funk CD, Hoshiko S, Matsumoto T, Rdmark O, Samuelsson B: Characterization of the human 5-lipoxygenase gene. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2587-91. [PubMed Link Image]
  7. Hoshiko S, Radmark O, Samuelsson B: Characterization of the human 5-lipoxygenase gene promoter. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9073-7. [PubMed Link Image]
  8. Rouzer CA, Samuelsson B: Reversible, calcium-dependent membrane association of human leukocyte 5-lipoxygenase. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7393-7. [PubMed Link Image]
  9. Nguyen T, Falgueyret JP, Abramovitz M, Riendeau D: Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase. J Biol Chem. 1991 Nov 15;266(32):22057-62. [PubMed Link Image]
  10. Ishii S, Noguchi M, Miyano M, Matsumoto T, Noma M: Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase. Biochem Biophys Res Commun. 1992 Feb 14;182(3):1482-90. [PubMed Link Image]
  11. Woods JW, Evans JF, Ethier D, Scott S, Vickers PJ, Hearn L, Heibein JA, Charleson S, Singer II: 5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes. J Exp Med. 1993 Dec 1;178(6):1935-46. [PubMed Link Image]
  12. Werz O, Szellas D, Steinhilber D, Radmark O: Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2). J Biol Chem. 2002 Apr 26;277(17):14793-800. Epub 2002 Feb 13. [PubMed Link Image]
  13. Luo M, Jones SM, Phare SM, Coffey MJ, Peters-Golden M, Brock TG: Protein kinase A inhibits leukotriene synthesis by phosphorylation of 5-lipoxygenase on serine 523. J Biol Chem. 2004 Oct 1;279(40):41512-20. Epub 2004 Jul 26. [PubMed Link Image]
  14. Flamand N, Lefebvre J, Surette ME, Picard S, Borgeat P: Arachidonic acid regulates the translocation of 5-lipoxygenase to the nuclear membranes in human neutrophils. J Biol Chem. 2006 Jan 6;281(1):129-36. Epub 2005 Nov 7. [PubMed Link Image]
  15. Strid T, Svartz J, Franck N, Hallin E, Ingelsson B, Soderstrom M, Hammarstrom S: Distinct parts of leukotriene C(4) synthase interact with 5-lipoxygenase and 5-lipoxygenase activating protein. Biochem Biophys Res Commun. 2009 Apr 17;381(4):518-22. Epub 2009 Feb 20. [PubMed Link Image]
  16. Flamand N, Luo M, Peters-Golden M, Brock TG: Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export. J Biol Chem. 2009 Jan 2;284(1):306-13. Epub 2008 Nov 1. [PubMed Link Image]
  17. Goodman JE, Bowman ED, Chanock SJ, Alberg AJ, Harris CC: Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk. Carcinogenesis. 2004 Dec;25(12):2467-72. Epub 2004 Aug 12. [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