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Human Metabolome Database Version 2.5

 

Showing metabocard for Geranyl-PP (HMDB01285)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:39
Accession Number HMDB01285
Secondary Accession Numbers HMDB01560; HMDB02239
Common Name Geranyl-PP
Description Geranyl diphosphate is the precursor of monoterpenes, a large family of natural occurring C10 compounds predominately found in plants and animals. Geranyl diphosphate is regarded as a key intermediate in the steroid, isoprene and terpene biosynthesis pathways and is used by organisms in the biosynthesis of farnesyl pyrophosphate, geranylgeranyl pyrophosphate, cholesterol, terpenes and terpenoids. (wikipedia). In humans, geranyl diphosphate synthase (GPPS) catalyzes the condensation of dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) to form geranyl diphosphate. Animals produce IPP through the mevalonate (MVA) pathway. Isoprenoid compounds have been implicated in several human disease states including coronary heart disease, blindness, infectious hepatitis and cancer. Geranyl pyrophosphate is an intermediate in the HMG-CoA reductase pathway used by organisms in the biosynthesis of terpenes and terpenoids. -- Wikipedia
Synonyms
  1. geranyl-PP
  2. Neryl diphosphate
  3. geranyl-diphosphate
  4. geranyl-pyrophosphate
  5. Monoterpenyl diphosphate
  6. geranyl diphosphate
  7. (2E)-3,7-dimethylocta-2,6-dien-1-yl trihydrogen diphosphate
  8. Geranyl pyrophosphic acid
  9. trans-geranyl pyrophosphate
Chemical IUPAC Name 3,7-dimethylocta-2,6-dienyl phosphono hydrogen phosphate
Chemical Formula C10H20O7P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Medium chain acyl phosphates
Family
  • Mammalian Metabolite
Species
  • phosphoric acid ester
  • alkene
Biofunction
  • Component of Terpenoid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 314.209
Monoisotopic Molecular Weight 314.068420
Isomeric SMILES CC(C)=CCCC(C)=CCOP(O)(=O)OP(O)(O)=O
Canonical SMILES CC(C)=CCCC(C)=CCOP(O)(=O)OP(O)(O)=O
KEGG Compound ID C00341 Link Image
BioCyc ID GERANYL-PP Link Image
BiGG ID 34712 Link Image
Wikipedia Link Geranyl pyrophosphate Link Image
NuGOwiki Link HMDB01285 Link Image
Metagene Link HMDB01285 Link Image
METLIN ID 6134 Link Image
PubChem Compound 445995 Link Image
PubChem Substance 14759890 Link Image
ChEBI ID 17211 Link Image
CAS Registry Number 763-10-0
InChI Identifier InChI=1/C10H20O7P2/c1-9(2)5-4-6-10(3)7-8-16-19(14,15)17-18(11,12)13/h5,7H,4,6,8H2,1-3H3,(H,14,15)(H2,11,12,13)/b10-7+
Synthesis Reference Runquist M; Ericsson J; Thelin A; Chojnacki T; Dallner G Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues. Biochemical and biophysical research communications (1992), 186(1), 157-65.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.90200007 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.63 [Predicted by ALOGPS]; 1.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
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 Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Micali E, Chehade KA, Isaacs RJ, Andres DA, Spielmann HP: Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Biochemistry. 2001 Oct 16;40(41):12254-65. [PubMed Link Image]
  2. Kavanagh KL, Guo K, Dunford JE, Wu X, Knapp S, Ebetino FH, Rogers MJ, Russell RG, Oppermann U: The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs. Proc Natl Acad Sci U S A. 2006 May 16;103(20):7829-34. Epub 2006 May 9. [PubMed Link Image]
  3. Holstein SA, Hohl RJ: Isoprenoids: remarkable diversity of form and function. Lipids. 2004 Apr;39(4):293-309. [PubMed Link Image]
  4. Gan X, Kaplan R, Menke JG, MacNaul K, Chen Y, Sparrow CP, Zhou G, Wright SD, Cai TQ: Dual mechanisms of ABCA1 regulation by geranylgeranyl pyrophosphate. J Biol Chem. 2001 Dec 28;276(52):48702-8. Epub 2001 Oct 18. [PubMed Link Image]
  5. Sagami H, Ogura K: [A new development in isoprenoid biochemistry brought by the discovery of prenylated proteins] Seikagaku. 1994 Dec;66(12):1488-501. [PubMed Link Image]
  6. Loza-Tavera H: Monoterpenes in essential oils. Biosynthesis and properties. Adv Exp Med Biol. 1999;464:49-62. [PubMed Link Image]
  7. Barnard GF, Popjak G: Human liver prenyltransferase and its characterization. Biochim Biophys Acta. 1981 Sep 15;661(1):87-99. [PubMed Link Image]
  8. Pont F, Luciani B, Belmant C, Fournie JJ: Characterization of phosphoantigens by high-performance anion-exchange chromatography-electrospray ionization ion trap mass spectrometry and nanoelectrospray ionization ion trap mass spectrometry. Anal Chem. 2001 Aug 1;73(15):3562-9. [PubMed Link Image]
  9. Smit A, Mushegian A: Biosynthesis of isoprenoids via mevalonate in Archaea: the lost pathway. Genome Res. 2000 Oct;10(10):1468-84. [PubMed Link Image]
  10. Wikipedia Link Image
Metabolic Enzymes
  1. Geranylgeranyl pyrophosphate synthetase
  2. Farnesyl pyrophosphate synthetase
  3. Farnesyl diphosphate synthase
Enzyme 1 [top]
Enzyme 1 ID 6219
Enzyme 1 Name Geranylgeranyl pyrophosphate synthetase
Enzyme 1 Synonyms
  1. GGPP synthetase
  2. GGPPSase
  3. Geranylgeranyl diphosphate synthase[Includes: Dimethylallyltranstransferase
Enzyme 1 Gene Name GGPS1
Enzyme 1 Protein Sequence >Geranylgeranyl pyrophosphate synthetase 
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNAS
LLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLL
ELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTL
GLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTEN
IDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
Enzyme 1 Number of Residues 300
Enzyme 1 Molecular Weight 34871
Enzyme 1 Theoretical pI 6.06
Enzyme 1 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins
Enzyme 1 Pathways
Enzyme 1 Reactions
  • trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4520350 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O95749 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GGPPS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >903 bp 
ATGGAGAAGACTCAAGAAACAGTCCAAAGAATTCTTCTAGAACCCTATAAATACTTACTT
CAGTTACCAGGTAAACAAGTGAGAACCAAACTTTCACAGGCATTTAATCATTGGCTGAAA
GTTCCAGAGGACAAGCTACAGATTATTATTGAAGTGACAGAAATGTTGCATAATGCCAGT
TTACTCATCGATGATATTGAAGACAACTCAAAACTCCGACGTGGCTTTCCAGTGGCCCAC
AGCATCTATGGAATCCCATCTGTCATCAATTCTGCCAATTACGTGTATTTCCTTGGCTTG
GAGAAAGTCTTAACCCTTGATCACCCAGATGCAGTGAAGCTTTTTACCCGCCAGCTTTTG
GAACTCCATCAGGGACAAGGCCTAGATATTTACTGGAGGGATAATTACACTTGTCCCACT
GAAGAAGAATATAAAGCTATGGTGCTGCAGAAAACAGGTGGACTGTTTGGATTAGCAGTA
GGTCTCATGCAGTTGTTCTCTGATTACAAAGAAGATTTAAAACCGCTACTTAATACACTT
GGGCTCTTTTTCCAAATTAGGGATGATTATGCTAATCTACACTCCAAAGAATATAGTGAA
AACAAAAGTTTTTGTGAAGATCTGACAGAGGGAAAGTTCTCATTTCCTACTATTCATGCT
ATTTGGTCAAGGCCTGAAAGCACCCAGGTGCAGAATATCTTGCGCCAGAGAACAGAAAAC
ATAGATATAAAAAAATACTGTGTACATTATCTTGAGGATGTAGGTTCTTTTGAATACACT
CGTAATACCCTTAAAGAGCTTGAAGCTAAAGCCTATAAACAGATTGATGCACGTGGTGGG
AACCCTGAGCTAGTAGCCTTAGTAAAACACTTAAGTAAGATGTTCAAAGAAGAAAATGAA
TAA
Enzyme 1 GenBank Gene ID AB017971 Link Image
Enzyme 1 GeneCard ID GGPS1 Link Image
Enzyme 1 GenAtlas ID GGPS1 Link Image
Enzyme 1 HGNC ID HGNC:4249 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1q43
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ericsson J, Greene JM, Carter KC, Shell BK, Duan DR, Florence C, Edwards PA: Human geranylgeranyl diphosphate synthase: isolation of the cDNA, chromosomal mapping and tissue expression. J Lipid Res. 1998 Sep;39(9):1731-9. [PubMed Link Image]
  2. Kuzuguchi T, Morita Y, Sagami I, Sagami H, Ogura K: Human geranylgeranyl diphosphate synthase. cDNA cloning and expression. J Biol Chem. 1999 Feb 26;274(9):5888-94. [PubMed Link Image]
  3. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  4. Kainou T, Kawamura K, Tanaka K, Matsuda H, Kawamukai M: Identification of the GGPS1 genes encoding geranylgeranyl diphosphate synthases from mouse and human. Biochim Biophys Acta. 1999 Mar 25;1437(3):333-40. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6220
Enzyme 2 Name Farnesyl pyrophosphate synthetase
Enzyme 2 Synonyms
  1. FPP synthetase
  2. FPS
  3. Farnesyl diphosphate synthetase[Includes: Dimethylallyltranstransferase
Enzyme 2 Gene Name FDPS
Enzyme 2 Protein Sequence >Farnesyl pyrophosphate synthetase 
MNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNR
GLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQICWYQ
KPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLDLLTAPQ
GNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQ
IQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVAR
VKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
Enzyme 2 Number of Residues 353
Enzyme 2 Molecular Weight 40533
Enzyme 2 Theoretical pI 4.80
Enzyme 2 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 202-219
  • 322-344
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 182399 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P14324 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name FPPS_HUMAN Link Image
Enzyme 2 PDB ID 1YV5 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1062 bp 
ATGAACGGAGACCAGAATTCAGATGTTTATGCCCAAGAAAAGCAGGATTTCGTTCAGCAC
TTCTCCCAGATCGTTAGGGTGCTGACTGAGGATGAGATGGGGCACCCAGAGATAGGAGAT
GCTATTGCCCGGCTCAAGGAGGTCCTGGAGTACAATGCCATTGGAGGCAAGTATAACCGG
GGTTTGACGGTGGTAGTAGCATTCCGGGAGCTGGTGGAGCCAAGGAAACAGGATGCTGAT
AGTCTCCAGCGGGCCTGGACTGTGGGCTGGTGTGTGGAACTGCTGCAAGCTTTCTTCCTG
GTGGCAGATGACATCATGGATTCATCCCTTACCCGCCGGGGACAGACCTGCTGGTATCAG
AAGCCGGGCGTGGGTTTGGATGCCATCAATGATGCTAACCTCCTGGAAGCATGTATCTAC
CGCCTGCTGAAGCTCTATTGCCGGGAGCAGCCCTATTACCTGAACCTGATCGAGCTCTTC
CTGCAGAGTTCCTATCAGACTGAGATTGGGCAGACCCTGGACCTCCTCACAGCCCCCCAG
GGCAATGTGGATCTTGTCAGATTCACTGAAAAGAGGTACAAATCTATTGTCAAGTACAAG
ACAGCTTTCTACTCCTTCTACCTTCCTATAGCTGCAGCCATGTACATGGCAGGAATTGAT
GGCGAGAAGGAGCACGCCAATGCCAAGAAGATCCTGCTGGAGATGGGGGAGTTCTTTCAG
ATTCAGGATGATTACCTTGACCTCTTTGGGGACCCCAGTGTGACCGGCAAAATTGGCACT
GACATCCAGGACAACAAATGCAGCTGGCTGGTGGTTCAGTGTCTGCAACGGGCCACTCCA
GAACAGTACCAGATCCTGAAGGAAAATTACGGGCAGAAGGAGGCTGAGAAAGTGGCCCGG
GTGAAGGCGCTATATGAGGAGCTGGATCTGCCAGCAGTGTTCTTGCAATATGAGGAAGAC
AGTTACAGCCACATTATGGCTCTCATTGAACAGTACGCAGCACCCCTGCCCCCAGCCGTC
TTTCTGGGGCTTGCGCGCAAAATCTACAAGCGGAGAAAGTGA
Enzyme 2 GenBank Gene ID J05262 Link Image
Enzyme 2 GeneCard ID FDPS Link Image
Enzyme 2 GenAtlas ID FDPS Link Image
Enzyme 2 HGNC ID HGNC:3631 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1q22
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Wilkin DJ, Kutsunai SY, Edwards PA: Isolation and sequence of the human farnesyl pyrophosphate synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by phorbol ester. J Biol Chem. 1990 Mar 15;265(8):4607-14. [PubMed Link Image]
  2. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  3. Sheares BT, White SS, Molowa DT, Chan K, Ding VD, Kroon PA, Bostedor RG, Karkas JD: Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells. Biochemistry. 1989 Oct 3;28(20):8129-35. [PubMed Link Image]
  4. Lefebvre L, Vanderplasschen A, Ciminale V, Heremans H, Dangoisse O, Jauniaux JC, Toussaint JF, Zelnik V, Burny A, Kettmann R, Willems L: Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase. J Virol. 2002 Feb;76(3):1400-14. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13006
Enzyme 3 Name Farnesyl diphosphate synthase
Enzyme 3 Synonyms
  1. Farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
  2. Farnesyl diphosphate synthase
  3. Farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase, isoform CRA_b
  4. cDNA FLJ76177, highly similar to Homo sapiens farnesyl diphosphate synthase
  5. farnesyl pyrophosphate synthetase, dimethylallyltranstransferase, geranyltranstransferase
  6. FDPS, mRNA
Enzyme 3 Gene Name FDPS
Enzyme 3 Protein Sequence >Farnesyl diphosphate synthase 
MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAWHSARCWCQAWTEEPRA
LCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAI
GGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQTLD
LLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANAKKILLE
MGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKE
AEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
Enzyme 3 Number of Residues 419
Enzyme 3 Molecular Weight 48276
Enzyme 3 Theoretical pI 6.02
Enzyme 3 GO Classification
Function
—
Process
  • cellular lipid metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 14603061 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96G29 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q96G29_HUMAN Link Image
Enzyme 3 PDB ID 1YV5 Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID BC010004 Link Image
Enzyme 3 GeneCard ID Q96G29 Link Image
Enzyme 3 GenAtlas ID FDPS Link Image
Enzyme 3 HGNC ID HGNC:3631 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available