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Human Metabolome Database Version 2.5

 

Showing metabocard for Presqualene diphosphate (HMDB01278)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-05-07 09:22:33
Accession Number HMDB01278
Secondary Accession Numbers Not Available
Common Name Presqualene diphosphate
Description Presqualene diphosphate is an intermediate in the biosynthesis of Terpenoid. It is a substrate for Farnesyl-diphosphate farnesyltransferase.
Synonyms
  1. (1alpha,2beta(E),3beta(1E,5E))-Diphosphoric acid mono((2-(4,8-dimethyl-3,7-nonadienyl)-2-methyl-3-(2,6,10-trimethyl-1,5,9-undecatrienyl)cyclopropyl)methyl) ester
  2. Presqualene diphosphate
  3. Presqualene diphosphic acid
  4. Presqualene pyrophosphate
Chemical IUPAC Name [[2-(4,8-dimethylnona-3,7-dienyl)-2-methyl-3-(2,6,10-trimethylundeca-1,5,9-trienyl)cyclopropyl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid
Chemical Formula C30H52O7P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Long chain acyl phosphates
Family
  • Mammalian Metabolite
Species
  • phosphoric acid ester
  • alkene
Biofunction
  • Component of Terpenoid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 586.677
Monoisotopic Molecular Weight 586.318848
Isomeric SMILES CC(C)=CCCC(C)=CCCC(C)=C[C@H]1[C@H](COP(O)(=O)OP(O)(O)=O)[C@@]1(C)CCC=C(/C)CCC=C(C)C
Canonical SMILES CC(C)=CCCC(C)=CCCC(C)=CC1C(COP(O)(=O)OP(O)(O)=O)C1(C)CCC=C(C)CCC=C(C)C
KEGG Compound ID C03428 Link Image
BioCyc ID CPD-465 Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB01278 Link Image
Metagene Link HMDB01278 Link Image
METLIN ID 6132 Link Image
PubChem Compound 6449797 Link Image
PubChem Substance 11971994 Link Image
ChEBI ID 15442 Link Image
CAS Registry Number 29849-75-0
InChI Identifier InChI=1/C30H52O7P2/c1-23(2)13-9-15-25(5)17-11-18-27(7)21-28-29(22-36-39(34,35)37-38(31,32)33)30(28,8)20-12-19-26(6)16-10-14-24(3)4/h13-14,17,19,21,28-29H,9-12,15-16,18,20,22H2,1-8H3,(H,34,35)(H2,31,32,33)/b25-17+,26-19+,27-21+/t28-,29-,30-/m0/s1
Synthesis Reference Rogers, Daniel H.; Yi, Eugene C.; Poulter, C. Dale. Enantioselective Synthesis of (+)-Presqualene Diphosphate. Journal of Organic Chemistry (1995), 60(4), 941-5.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.14e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5.31 [Predicted by ALOGPS]; 4.838 [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 Not Available
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 Not Available
Metabolic Enzymes
  1. Squalene synthase
Enzyme 1 [top]
Enzyme 1 ID 5492
Enzyme 1 Name Squalene synthase
Enzyme 1 Synonyms
  1. SQS
  2. SS
  3. FPP:FPP farnesyltransferase
  4. Farnesyl-diphosphate farnesyltransferase
Enzyme 1 Gene Name FDFT1
Enzyme 1 Protein Sequence >Squalene synthase 
MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
Enzyme 1 Number of Residues 417
Enzyme 1 Molecular Weight 48114.9
Enzyme 1 Theoretical pI 6.51
Enzyme 1 GO Classification
Function
  • catalytic activity
  • farnesyl-diphosphate farnesyltransferase activity
  • farnesyltranstransferase activity
  • prenyltransferase activity
  • transferase activity
  • transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
  • biosynthetic process
  • lipid biosynthetic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 1 General Function Involved in transferase activity
Enzyme 1 Specific Function 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) (1a) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate [RN:R00702]
  • (2) (1b) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+ [RN:R02872]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 284-304 384-404
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID P37268 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name FDFT_HUMAN Link Image
Enzyme 1 PDB ID 1EZF Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1254 bp 
ATGGAGTTCGTGAAATGCCTTGGCCACCCCGAAGAGTTCTACAACCTGGTGCGCTTCCGG
ATCGGGGGCAAGCGGAAGGTGATGCCCAAGATGGACCAGGACTCGCTCAGCAGCAGCCTG
AAAACTTGCTACAAGTATCTCAATCAGACCAGTCGCAGTTTCGCAGCTGTTATCCAGGCG
CTGGATGGGGAAATGCGCAACGCAGTGTGCATATTTTATCTGGTTCTCCGAGCTCTGGAC
ACACTGGAAGATGACATGACCATCAGTGTGGAAAAGAAGGTCCCGCTGTTACACAACTTT
CACTCTTTCCTTTACCAACCAGACTGGCGGTTCATGGAGAGCAAGGAGAAGGATCGCCAG
GTGCTGGAGGACTTCCCAACGATCTCCCTTGAGTTTAGAAATCTGGCTGAGAAATACCAA
ACAGTGATTGCCGACATTTGCCGGAGAATGGGCATTGGGATGGCAGAGTTTTTGGATAAG
CATGTGACCTCTGAACAGGAGTGGGACAAGTACTGCCACTATGTTGCTGGGCTGGTCGGA
ATTGGCCTTTCCCGTCTTTTCTCAGCCTCAGAGTTTGAAGACCCCTTAGTTGGTGAAGAT
ACAGAACGTGCCAACTCTATGGGCCTGTTTCTGCAGAAAACAAACATCATCCGTGACTAT
CTGGAAGACCAGCAAGGAGGAAGAGAGTTCTGGCCTCAAGAGGTTTGGAGCAGGTATGTT
AAGAAGTTAGGGGATTTTGCTAAGCCGGAGAATATTGACTTGGCCGTGCAGTGCCTGAAT
GAACTTATAACCAATGCACTGCACCACATCCCAGATGTCATCACCTACCTTTCGAGACTC
AGAAACCAGAGTGTGTTTAACTTCTGCGCTATTCCACAGGTGATGGCCATTGCCACTTTG
GCTGCCTGTTATAATAACCAGCAGGTGTTCAAAGGGGCAGTGAAGATTCGGAAAGGGCAA
GCAGTGACCCTGATGATGGATGCCACCAATATGCCAGCTGTCAAAGCCATCATATATCAG
TATATGGAAGAGATTTATCATAGAATCCCCGACTCAGACCCATCTTCTAGCAAAACAAGG
CAGATCATCTCCACCATCCGGACGCAGAATCTTCCCAACTGTCAGCTGATTTCCCGAAGC
CACTACTCCCCCATCTACCTGTCGTTTGTCATGCTTTTGGCTGCCCTGAGCTGGCAGTAC
CTGACCACTCTCTCCCAGGTAACAGAAGACTATGTTCAGACTGGAGAACACTGA
Enzyme 1 GenBank Gene ID L06070 Link Image
Enzyme 1 GeneCard ID FDFT1 Link Image
Enzyme 1 GenAtlas ID FDFT1 Link Image
Enzyme 1 HGNC ID HGNC:3629 Link Image
Enzyme 1 Chromosome Location 8
Enzyme 1 Locus 8p23.1-p22
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW: Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol Cell Biol. 1993 May;13(5):2706-17. [PubMed Link Image]
  2. Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem. 1993 Jun 15;268(17):12818-24. [PubMed Link Image]
  3. Summers C, Karst F, Charles AD: Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 1993 Dec 22;136(1-2Che):185-92. [PubMed Link Image]
  4. Soltis DA, McMahon G, Caplan SL, Dudas DA, Chamberlin HA, Vattay A, Dottavio D, Rucker ML, Engstrom RG, Cornell-Kennon SA, et al.: Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. Arch Biochem Biophys. 1995 Feb 1;316(2):713-23. [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. Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ Jr: Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J Biol Chem. 2000 Sep 29;275(39):30610-7. [PubMed Link Image]
  7. Do R, Pare G, Montpetit A, Hudson TJ, Gaudet D, Engert JC: K45R variant of squalene synthase increases total cholesterol levels in two study samples from a French Canadian population. Hum Mutat. 2008 May;29(5):689-94. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available