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Human Metabolome Database Version 2.5

 

Showing metabocard for Leukotriene F4 (HMDB06465)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-23 11:28:31
Update Date 2009-05-05 21:01:01
Accession Number HMDB06465
Secondary Accession Numbers HMDB04414; HMDB05075
Common Name Leukotriene F4
Description Leukotriene F4 is an intermediate in Arachidonic acid metabolism. Leukotriene F4 is converted from Leukotriene E4 via the enzyme Transferases (EC 2.3.2.-). 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. LTF4
  2. 5S-hydroxy-6R-(S-glutamylcysteinyl)-7E,9E,11Z,14Z-eicosatetraenoic acid
  3. 5S-hydroxy-6R-(S-glutamylcysteinyl)-7E,9E,11Z,14Z-eicosatetraenoate
Chemical IUPAC Name (5S,6R,7E,9E,11Z, 14Z)-6-[(2R)-2-[[(4S)-4-amino-5-hydroxy-5-oxopentanoyl]amino]-3-hydroxy- 3-oxopropyl]sulfanyl-5-hydroxyicosa-7,9,11,14-tetraenoic acid
Chemical Formula C28H44N2O8S
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Fatty acids
Class
  • Eicosanoids
Sub Class
  • Leukotrienes
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • thioether
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • alkene
  • alpha-aminoacid
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 568.723
Monoisotopic Molecular Weight 568.281860
Isomeric SMILES CCCCCC=C/CC=C/C=C/C=C/[C@@H](SC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(O)=O)[C@@H](O)CCCC(O)=O
Canonical SMILES CCCCCC=CCC=CC=CC=CC(SCC(NC(=O)CCC(N)C(O)=O)C(O)=O)C(O)CCCC(O)=O
KEGG Compound ID C06462 Link Image
BioCyc ID Not Available
BiGG ID 2705818 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB06465 Link Image
Metagene Link HMDB06465 Link Image
METLIN ID Not Available
PubChem Compound 5280938 Link Image
PubChem Substance 24583222 Link Image
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C28H44N2O8S/c1-2-3-4-5-6-7-8-9-10-11-12-13-16-24(23(31)15-14-17-26(33)34)39-20-22(28(37)38)30-25(32)19-18-21(29)27(35)36/h6-7,9-13,16,21-24,31H,2-5,8,14-15,17-20,29H2,1H3,(H,30,32)(H,33,34)(H,35,36)(H,37,38)/b7-6-,10-9-,12-11+,16-13+/t21-,22-,23-,24+/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.95e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.69 [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
  • Cytoplasm
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.000305 +/- 0.000069 uM
Age Adult:>18 yrs old
Sex Both
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]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways Not Available
General References Not Available
Metabolic Enzymes
  1. Gamma-glutamyltranspeptidase 1
  2. Gamma-glutamyltransferase 7
  3. Gamma-glutamyltransferase 6
Enzyme 1 [top]
Enzyme 1 ID 6005
Enzyme 1 Name Gamma-glutamyltranspeptidase 1
Enzyme 1 Synonyms
  1. GGT 1
  2. Gamma-glutamyltransferase 1
  3. CD224 antigen
  4. Gamma-glutamyltranspeptidase 1 heavy chain
  5. Gamma-glutamyltranspeptidase 1 light chain
Enzyme 1 Gene Name GGT1
Enzyme 1 Protein Sequence >Gamma-glutamyltranspeptidase 1
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY
Enzyme 1 Number of Residues 569
Enzyme 1 Molecular Weight 61409.7
Enzyme 1 Theoretical pI 7.14
Enzyme 1 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 1 General Function Involved in gamma-glutamyltransferase activity
Enzyme 1 Specific Function Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 5-26
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 183138 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P19440 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GGT1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1710 bp
ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA
Enzyme 1 GenBank Gene ID J04131 Link Image
Enzyme 1 GeneCard ID GGT1 Link Image
Enzyme 1 GenAtlas ID GGT1 Link Image
Enzyme 1 HGNC ID HGNC:4250 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 22q11.23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed Link Image]
  2. Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed Link Image]
  3. Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed Link Image]
  4. Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed Link Image]
  5. Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed Link Image]
  6. Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed Link Image]
  7. Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed Link Image]
  8. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  9. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  10. 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]
  11. Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed Link Image]
  12. Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed Link Image]
  13. Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed Link Image]
  14. Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed Link Image]
  15. Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed Link Image]
  16. Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed Link Image]
  17. Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed Link Image]
  18. Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed Link Image]
  19. Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A: A proteomic analysis of human bile. Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14. [PubMed Link Image]
  20. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  21. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
Enzyme 1 Metabolite References
  1. Hammarstrom S, Orning L, Bernstrom K: Metabolism of leukotrienes. Mol Cell Biochem. 1985 Nov;69(1):7-16. [PubMed Link Image]
Enzyme 2 [top]
Enzyme 2 ID 6006
Enzyme 2 Name Gamma-glutamyltransferase 7
Enzyme 2 Synonyms
  1. GGT 7
  2. Gamma-glutamyltransferase-like 3
  3. Gamma-glutamyltransferase-like 5
  4. Gamma-glutamyltranspeptidase 7
  5. Gamma-glutamyltransferase 7 heavy chain
  6. Gamma-glutamyltransferase 7 light chain
Enzyme 2 Gene Name GGT7
Enzyme 2 Protein Sequence >Gamma-glutamyltransferase 7
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDS
FLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATG
VTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPH
SSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLH
EAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPL
PGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEK
PVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
RLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMG
PDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPL
SFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLARGRLHPDL
QSNLLQVDSEFTEEEIEFLEARGHHVEKVDVLSWVHGSRRTNNFIIAVKDPRSPDAAGAT
IL
Enzyme 2 Number of Residues 662
Enzyme 2 Molecular Weight 70466.0
Enzyme 2 Theoretical pI 4.73
Enzyme 2 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 2 General Function Involved in gamma-glutamyltransferase activity
Enzyme 2 Specific Function Cleaves glutathione conjugates
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 107-127
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 109148539 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9UJ14 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name GGT7_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1989 bp
ATGGCGGCGGAGAACGAGGCCAGCCAGGAGAGCGCCCTGGGCGCCTACTCGCCAGTGGAC
TACATGAGCATCACCAGCTTCCCGCGGCTGCCCGAGGACGAGCCGGCGCCCGCGGCCCCG
CTGAGGGGCCGCAAGGACGAGGACGCCTTTCTGGGAGACCCCGACACCGACCCGGACTCC
TTCCTGAAGTCTGCACGGCTGCAGCGGCTGCCATCGTCGTCGTCGGAGATGGGCAGCCAA
GACGGGTCGCCGCTACGCGAGACGCGCAAAGACCCGTTCTCCGCCGCAGCGGCCGAGTGC
TCCTGCCGCCAGGATGGGCTCACGGTCATCGTCACGGCCTGTCTCACCTTCGCTACCGGT
GTCACCGTGGCGCTGGTCATGCAGATCTACTTCGGGGACCCCCAGATCTTCCAGCAGGGT
GCCGTGGTGACCGATGCTGCCCGCTGCACTTCACTGGGCATCGAGGTGCTCAGTAAACAG
GGATCTTCTGTGGACGCAGCGGTGGCAGCAGCCTTGTGTTTGGGTATCGTGGCTCCACAC
AGTTCTGGCCTGGGCGGTGGGGGCGTGATGCTGGTACATGACATCCGACGAAATGAGAGC
CACCTAATTGATTTCCGGGAGTCCGCACCAGGGGCCCTCAGGGAAGAGACCCTGCAAAGA
TCCTGGGAGACCAAGCCTGGGCTCTTGGTGGGGGTTCCCGGAATGGTGAAGGGGCTACAT
GAAGCTCACCAGCTCTATGGCAGGCTGCCATGGTCCCAAGTCCTGGCCTTTGCAGCAGCT
GTGGCCCAAGATGGCTTCAACGTGACTCATGATCTAGCCCGTGCCCTGGCTGAACAGCTG
CCACCCAACATGTCCGAGCGCTTCCGGGAGACGTTCCTGCCATCGGGCCGCCCGCCACTA
CCTGGCTCGTTGCTGCATCGGCCCGACCTGGCTGAGGTGCTGGATGTACTTGGCACCTCC
GGCCCGGCTGCCTTCTACGCAGGTGGCAACCTCACACTGGAGATGGTGGCCGAGGCTCAG
CACGCAGGGGGTGTCATAACCGAAGAGGACTTCAGCAATTACAGCGCCCTTGTGGAGAAG
CCTGTGTGTGGCGTGTACAGAGGCCACCTGGTTCTTAGTCCCCCACCTCCGCACACGGGC
CCTGCCCTCATCAGTGCTCTCAACATCCTGGAGGGCTTCAATCTCACCAGCCTGGTATCC
CGAGAACAGGCTCTTCACTGGGTGGCAGAGACCCTGAAGATTGCATTAGCCCTGGCCAGC
AGACTGGGAGATCCCGTCTATGATTCTACCATCACTGAGAGCATGGATGACATGCTCAGC
AAGGTGGAGGCCGCCTACCTCCGGGGCCATATCAATGACTCCCAGGCAGCCCCTGCCCCA
CTCCTGCCTGTCTATGAACTAGACGGAGCTCCCACGGCTGCCCAGGTGCTGATCATGGGA
CCTGATGACTTCATTGTGGCCATGGTTAGCTCCCTGAACCAGCCCTTTGGCAGCGGCCTT
ATCACCCCCTCGGGGATCCTGCTCAACAGCCAGATGCTGGACTTCTCCTGGCCCAACCGG
ACAGCTAACCACTCTGCACCCAGCCTGGAGAATTCAGTGCAGCCAGGGAAGCGGCCACTC
TCTTTCCTGCTGCCCACAGTGGTCCGACCCGCGGAGGGGCTCTGTGGAACCTACCTCGCT
CTGGGGGCCAATGGAGCTGCGCGGGGCCTCAGCGGCCTGACACAGGTTCTGCTGAATGTC
CTGACCTTGAACCGGAACCTGAGTGACAGCCTGGCCCGCGGCCGCCTACACCCGGACCTG
CAGTCCAACCTCCTGCAGGTGGACAGTGAGTTCACAGAGGAAGAGATTGAGTTCCTGGAA
GCCAGGGGTCACCACGTGGAGAAAGTAGATGTCTTATCCTGGGTCCATGGCAGCCGAAGG
ACCAACAACTTCATCATCGCTGTTAAGGACCCTCGGAGCCCAGATGCAGCTGGAGCCACC
ATCCTGTAG
Enzyme 2 GenBank Gene ID NM_178026.2 Link Image
Enzyme 2 GeneCard ID GGT7 Link Image
Enzyme 2 GenAtlas ID GGT7 Link Image
Enzyme 2 HGNC ID HGNC:4259 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 20q11.22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. He X, Di Y, Li J, Xie Y, Tang Y, Zhang F, Wei L, Zhang Y, Qin W, Huo K, Li Y, Wan D, Gu J: Molecular cloning and characterization of CT120, a novel membrane-associated gene involved in amino acid transport and glutathione metabolism. Biochem Biophys Res Commun. 2002 Sep 27;297(3):528-36. [PubMed Link Image]
  2. 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]
  3. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Heisterkamp N, Groffen J, Warburton D, Sneddon TP: The human gamma-glutamyltransferase gene family. Hum Genet. 2008 May;123(4):321-32. Epub 2008 Mar 21. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 2 Metabolite References
  1. Hammarstrom S, Orning L, Bernstrom K: Metabolism of leukotrienes. Mol Cell Biochem. 1985 Nov;69(1):7-16. [PubMed Link Image]
Enzyme 3 [top]
Enzyme 3 ID 12987
Enzyme 3 Name Gamma-glutamyltransferase 6
Enzyme 3 Synonyms
  1. GGT 6
  2. Gamma-glutamyltranspeptidase 6
  3. Gamma-glutamyltransferase 6 heavy chain
  4. Gamma-glutamyltransferase 6 light chain
Enzyme 3 Gene Name GGT6
Enzyme 3 Protein Sequence >Gamma-glutamyltransferase 6
MERAEEPVVYQKLLPWEPSLESEEEVEEEETSEALVLNPRRHQDSSRNKAGGLPGTWARV
VAALLLLAVGCSLAVRQLQNQGRSTGSLGSVAPPPGGHSHGPGVYHHGAIISPAGRELLV
AGGNVVDAGVGAALCLAVVHPHATGLGAMFWGLFHDSSSGNSTALTSGPAQTLAPGLGLP
AALPTLHLLHARFGRLPWPRLLVGPTTLAQEGFLVDTPLARALVARGTEGLCPLLCHADG
TPLGAGARATNPQLAAVLRSAALAPTSDLAGDALLSLLAGDLGVEVPSAVPRPTLEPAEQ
LPVPQGILFTTPSPSAGPELLALLEAALRSGAPIPDPCPPFLQTAVSPESSALAAVDSSG
SVLLLTSSLNCSFGSAHLSPSTGVLLSNLVAKSTTSAWACPLILRGSLDDTEADVLGLVA
SGTPDVARAMTHTLLRHLAARPPTQAQHQHQGQQEPTEHPSTCGQGTLLQVAAHTEHAHV
SSVPHACCPFQGF
Enzyme 3 Number of Residues 493
Enzyme 3 Molecular Weight 50508.8
Enzyme 3 Theoretical pI 6.04
Enzyme 3 GO Classification
Function
  • catalytic activity
  • gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
Component
Enzyme 3 General Function Involved in gamma-glutamyltransferase activity
Enzyme 3 Specific Function Cleaves glutathione conjugates
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 55-75
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 171543825 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q6P531 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GGT6_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1482 bp
ATGGAGCGGGCAGAAGAGCCCGTGGTCTATCAGAAGCTGCTGCCCTGGGAGCCAAGCTTG
GAGTCGGAGGAGGAAGTGGAGGAGGAGGAGACATCAGAGGCGCTGGTTCTAAACCCCCGG
AGGCACCAGGACTCTTCCAGGAACAAGGCTGGCGGGCTGCCCGGAACCTGGGCCCGTGTA
GTGGCAGCCCTGCTGCTGCTGGCTGTTGGCTGCTCCCTGGCTGTGAGGCAGCTCCAGAAT
CAGGGCAGGTCGACAGGAAGCTTGGGCTCTGTGGCCCCTCCACCCGGCGGACACTCCCAC
GGCCCTGGCGTATACCACCACGGTGCCATCATCAGCCCTGCAGGCCGAGAGCTGCTTGTT
GCCGGGGGCAACGTCGTGGATGCTGGAGTTGGAGCTGCATTGTGCCTGGCAGTGGTGCAT
CCTCATGCCACGGGGCTAGGTGCCATGTTTTGGGGCCTCTTCCACGATAGCTCCTCAGGC
AATTCCACGGCCCTGACATCAGGCCCAGCACAGACCCTGGCCCCCGGCCTGGGGCTGCCC
GCGGCTCTGCCCACCCTGCACCTGCTGCATGCACGCTTCGGCCGCCTGCCCTGGCCACGC
CTGCTAGTGGGCCCCACCACGCTGGCTCAGGAGGGCTTCCTGGTGGACACACCCCTGGCA
AGGGCTCTGGTGGCTCGGGGCACAGAAGGCCTCTGTCCACTACTTTGCCATGCTGATGGG
ACACCCCTGGGCGCTGGGGCCCGAGCCACCAACCCACAACTGGCAGCTGTGCTTCGCAGC
GCAGCCCTCGCTCCCACCTCAGACCTTGCTGGGGATGCTCTACTGAGTCTACTGGCGGGA
GACCTGGGGGTGGAGGTGCCCTCGGCTGTGCCCAGGCCCACTTTGGAACCAGCAGAGCAG
CTACCTGTGCCCCAGGGCATCCTGTTCACCACCCCCAGTCCCTCAGCTGGCCCAGAACTG
CTGGCACTGTTGGAGGCAGCCCTGCGCTCCGGGGCGCCCATCCCTGACCCCTGCCCACCG
TTCCTGCAGACTGCTGTGAGCCCCGAGAGCAGTGCCCTGGCCGCCGTGGACAGCAGCGGC
TCTGTGCTCCTTCTCACCTCCTCGCTCAACTGCTCCTTTGGCTCTGCACACCTGTCCCCA
AGCACTGGGGTTCTGCTCAGCAACCTGGTGGCCAAGTCTACCACTAGTGCCTGGGCCTGC
CCCCTCATCCTCCGTGGCAGCCTGGATGACACAGAGGCTGATGTGTTGGGGCTTGTGGCT
TCAGGGACCCCTGATGTGGCCAGGGCCATGACTCACACCCTACTCAGGCATCTGGCAGCA
AGGCCCCCTACCCAGGCCCAGCACCAGCATCAGGGTCAGCAAGAACCAACAGAGCATCCC
AGCACTTGTGGCCAAGGGACCCTGCTCCAGGTGGCAGCCCACACAGAGCACGCCCATGTC
TCCAGTGTCCCCCATGCCTGCTGCCCCTTCCAGGGGTTCTAA
Enzyme 3 GenBank Gene ID NM_001122890.1 Link Image
Enzyme 3 GeneCard ID GGT6 Link Image
Enzyme 3 GenAtlas ID GGT6 Link Image
Enzyme 3 HGNC ID HGNC:26891 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 17p13.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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]
  2. 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]
  3. Heisterkamp N, Groffen J, Warburton D, Sneddon TP: The human gamma-glutamyltransferase gene family. Hum Genet. 2008 May;123(4):321-32. Epub 2008 Mar 21. [PubMed Link Image]
Enzyme 3 Metabolite References
  1. Hammarstrom S, Orning L, Bernstrom K: Metabolism of leukotrienes. Mol Cell Biochem. 1985 Nov;69(1):7-16. [PubMed Link Image]