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Human Metabolome Database Version 2.5

 

Showing metabocard for 4,4-Dimethylcholesta-8,14,24-trienol (HMDB01023)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:29
Accession Number HMDB01023
Secondary Accession Numbers HMDB06924
Common Name 4,4-Dimethylcholesta-8,14,24-trienol
Description 4,4-Dimethylcholesta-8,14,24-trienol is a product of the enzyme delta14-sterol reductase [EC 1.3.1.70] (KEGG). It is involved in the biosynthesis of steroids and is involved in the conversion of lanosterol to zymosterol. In particular, lanosterol 14-alpha-demethylase, catalyzes the C-14 demethylation of lanosterol to form 4,4-Dimethylcholesta-8,14,24-trienol in the ergosterol biosynthesis pathway. It is thought to be a meiosis activating sterol.
Synonyms
  1. (3beta,5alpha)-4,4-Dimethylcholesta-8,14,24-trien-3-ol
  2. (3beta,5alpha)-4,4-dimethyl-Cholesta-8,14,24-trien-3-ol
  3. 4,4-Dimechol-8,14,24-trienol
  4. 4,4-Dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol
  5. 4,4-Dimethylcholesta-8,14,24-trienol
  6. 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
  7. 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol
  8. 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3-ol
  9. FF-MAS
  10. follicular fluid meiosis activating sterol
  11. 4,4-dimethyl-cholesta-8,14,24-trienol
Chemical IUPAC Name (3R,5S,10S,13S,17S)-4,4,10,13-tetramethyl-17-[(2R)-6-methylhept-5-en-2-yl]-1,2,3,5,6,7,11,12,16,17-decahydrocyclopenta[a]phenanthren-3-ol
Chemical Formula C29H46O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Miscellaneous steroids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • alkene
Biofunction
  • Hormones, Membrane component
Application
Source
  • Endogenous
Average Molecular Weight 410.675
Monoisotopic Molecular Weight 410.354858
Isomeric SMILES C[C@H](CCC=C(C)C)[C@H]1CC=C2C3=C(CC[C@]12C)[C@@]1(C)CC[C@H](O)C(C)(C)[C@@H]1CC3
Canonical SMILES CC(CCC=C(C)C)C1CC=C2C3=C(CCC12C)C1(C)CCC(O)C(C)(C)C1CC3
KEGG Compound ID C11455 Link Image
BioCyc ID 44-DIMETHYL-CHOLESTA-812-24-TRIENOL Link Image
BiGG ID 1454719 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01023 Link Image
Metagene Link HMDB01023 Link Image
METLIN ID 5952 Link Image
PubChem Compound 443212 Link Image
PubChem Substance 13626 Link Image
ChEBI ID 17813 Link Image
CAS Registry Number 64284-64-6
InChI Identifier InChI=1/C29H46O/c1-19(2)9-8-10-20(3)22-12-13-23-21-11-14-25-27(4,5)26(30)16-18-29(25,7)24(21)15-17-28(22,23)6/h9,13,20,22,25-26,30H,8,10-12,14-18H2,1-7H3/t20-,22-,25+,26+,28-,29-/m1/s1
Synthesis Reference Ruan B; Wilson W K; Schroepfer G J Jr An alternative synthesis of 4,4-dimethyl-5 alpha-cholesta-8,14,24-trien-3 beta-ol, an intermediate in sterol biosynthesis and a reported activator of meiosis and of nuclear orphan receptor LXR alpha. Bioorganic & medicinal chemistry letters (1998), 8(3), 233-6.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1.01e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 7.40 [Predicted by ALOGPS]; 6.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location Not Available
Tissue Location
Tissue References
Testes
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. Ruan B, Watanabe S, Eppig JJ, Kwoh C, Dzidic N, Pang J, Wilson WK, Schroepfer GJ Jr: Sterols affecting meiosis: novel chemical syntheses and the biological activity and spectral properties of the synthetic sterols. J Lipid Res. 1998 Oct;39(10):2005-20. [PubMed Link Image]
Metabolic Enzymes
  1. Delta(14)-sterol reductase
  2. Lanosterol 14-alpha demethylase
  3. Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5494
Enzyme 1 Name Delta(14)-sterol reductase
Enzyme 1 Synonyms
  1. Delta-14-SR
  2. Another new gene 1 protein
  3. C-14 sterol reductase
  4. Putative sterol reductase SR-1
  5. Sterol C14-reductase
  6. Transmembrane 7 superfamily member 2
Enzyme 1 Gene Name TM7SF2
Enzyme 1 Protein Sequence >Delta(14)-sterol reductase
MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSP
RALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAG
LPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELN
PRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWH
EEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATG
YYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALA
WSLPCGVSHLLPYFYLLYFTALLVHREARDERQCLQKYGLAWQEYCRRVPYRIMPYIY
Enzyme 1 Number of Residues 418
Enzyme 1 Molecular Weight 46405.3
Enzyme 1 Theoretical pI 9.04
Enzyme 1 GO Classification
Function
Process
Component
  • cell part
  • membrane
Enzyme 1 General Function Involved in delta14-sterol reductase activity
Enzyme 1 Specific Function Involved in the conversion of lanosterol to cholesterol
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP+ = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + NADPH + H+ [RN:R05639]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 13-35 62-81 102-124 129-148 255-277 287-304 355-377
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 117414150 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O76062 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ERG24_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1257 bp
ATGGCCCCCACTCAGGGCCCCCGGGCCCCGCTGGAATTCGGAGGGCCCCTGGGCGCCGCG
GCTCTGCTACTGCTGCTGCCCGCCACCATGTTCCACCTGCTCCTGGCGGCCCGTTCGGGC
CCCGCGCGCCTGCTGGGTCCACCCGCGTCCCTGCCCGGGCTGGAGGTGCTGTGGAGCCCA
CGGGCGCTGCTGCTGTGGCTCGCCTGGCTCGGCCTGCAGGCGGCGCTCTACCTACTGCCG
GCGCGCAAGGTGGCCGAGGGGCAGGAATTGAAGGACAAGAGTCGCCTGCGCTATCCTATT
AACGGCTTCCAGGCCCTGGTGCTGACAGCCCTGTTGGTGGGGCTGGGGATGTCAGCGGGG
CTGCCTCTGGGGGCGCTCCCGGAAATGCTCCTGCCCTTGGCGTTTGTCGCCACCCTCACC
GCTTTCATCTTCAGCCTCTTTCTCTACATGAAGGCGCAGGTAGCCCCAGTTTCGGCCCTG
GCACCTGGGGGGAACTCAGGCAATCCGATTTACGACTTTTTTCTGGGACGAGAGCTCAAC
CCTCGTATCTGTTTCTTCGACTTCAAATATTTCTGTGAACTGCGACCCGGCCTCATCGGC
TGGGTCCTCATCAACCTGGCCCTGTTGATGAAGGAGGCAGAGCTTCGAGGCAGTCCCTCA
CTGGCCATGTGGCTGGTCAATGGCTTCCAGTTGCTCTACGTGGGTGATGCCCTCTGGCAC
GAGGAGGCCGTCCTCACCACCATGGATATCACACATGACGGGTTTGGCTTCATGCTGGCG
TTTGGGGACATGGCCTGGGTGCCCTTCACCTACAGCCTGCAGGCCCAGTTCCTGCTGCAC
CACCCGCAGCCCCTGGGGTTGCCCATGGCCTCTGTCATCTGCCTCATCAATGCTACTGGT
TACTACATCTTCCGTGGGGCGAATTCCCAGAAAAACACTTTCCGAAAGAATCCTTCTGAC
CCCAGAGTGGCTGGGCTTGAGACCATCTCTACAGCCACAGGGCGGAAACTGCTGGTGTCT
GGGTGGTGGGGTATGGTCCGCCATCCCAACTATCTTGGAGACCTCATCATGGCTCTGGCT
TGGTCCTTGCCCTGCGGGGTGTCACACCTGCTGCCCTACTTCTACCTCCTCTACTTCACC
GCGCTGCTGGTGCACCGTGAGGCCCGGGATGAGCGGCAGTGCCTGCAGAAGTACGGCCTG
GCCTGGCAGGAGTACTGCCGGCGTGTGCCTTACCGCATCATGCCCTACATCTACTGA
Enzyme 1 GenBank Gene ID NM_003273.2 Link Image
Enzyme 1 GeneCard ID TM7SF2 Link Image
Enzyme 1 GenAtlas ID TM7SF2 Link Image
Enzyme 1 HGNC ID HGNC:11863 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 11q13
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Lemmens IH, Kas K, Merregaert J, Van de Ven WJ: Identification and molecular characterization of TM7SF2 in the FAUNA gene cluster on human chromosome 11q13. Genomics. 1998 May 1;49(3):437-42. [PubMed Link Image]
  2. Holmer L, Pezhman A, Worman HJ: The human lamin B receptor/sterol reductase multigene family. Genomics. 1998 Dec 15;54(3):469-76. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. 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. Roberti R, Bennati AM, Galli G, Caruso D, Maras B, Aisa C, Beccari T, Della Fazia MA, Servillo G: Cloning and expression of sterol Delta 14-reductase from bovine liver. Eur J Biochem. 2002 Jan;269(1):283-90. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5497
Enzyme 2 Name Lanosterol 14-alpha demethylase
Enzyme 2 Synonyms
  1. LDM
  2. CYPLI
  3. Cytochrome P450 51A1
  4. Cytochrome P450-14DM
  5. Cytochrome P45014DM
  6. Cytochrome P450LI
  7. Sterol 14-alpha demethylase
Enzyme 2 Gene Name CYP51A1
Enzyme 2 Protein Sequence >Lanosterol 14-alpha demethylase
MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKS
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNS
KNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETK
EYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWL
LPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDE
VAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDL
NLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLD
FNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFP
TVNYTTMIHTPENPVIRYKRRSK
Enzyme 2 Number of Residues 503
Enzyme 2 Molecular Weight 56805.3
Enzyme 2 Theoretical pI 8.72
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
Component
Enzyme 2 General Function Involved in monooxygenase activity
Enzyme 2 Specific Function Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O [RN:R05731]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 24-44
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 4503243 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q16850 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CP51A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1530 bp
ATGGCGGCGGCGGCTGGGATGCTGCTGCTGGGCTTGCTGCAGGCGGGTGGGTCGGTGCTG
GGCCAGGCGATGGAGAAGGTGACAGGCGGCAACCTCTTGTCCATGCTGCTGATCGCCTGC
GCCTTCACCCTCAGCCTGGTCTACCTGATCCGTCTGGCCGCCGGCCACCTGGTCCAGCTG
CCCGCAGGGGTGAAAAGTCCTCCATACATTTTCTCCCCAATTCCATTCCTTGGGCATGCC
ATAGCATTTGGGAAAAGTCCAATTGAATTTCTAGAAAATGCATATGAGAAGTATGGACCT
GTATTTAGTTTTACCATGGTAGGCAAGACATTTACTTACCTTCTGGGGAGTGATGCTGCT
GCACTGCTTTTTAATAGTAAAAATGAAGACCTGAATGCAGAAGATGTCTACAGTCGCCTG
ACAACACCTGTGTTTGGGAAGGGAGTTGCATACGATGTGCCTAATCCAGTTTTCTTGGAG
CAGAAGAAAATGTTAAAAAGTGGCCTTAACATAGCCCACTTTAAACAGCATGTTTCTATA
ATTGAAAAAGAAACAAAGGAATACTTTGAGAGTTGGGGAGAAAGTGGAGAAAAAAATGTG
TTTGAAGCTCTTTCTGAGCTCATAATTTTAACAGCTAGCCATTGTTTGCATGGAAAGGAA
ATCAGAAGTCAACTCAATGAAAAGGTAGCACAGCTGTATGCAGATTTGGATGGAGGTTTC
AGCCATGCAGCCTGGCTCTTACCAGGTTGGCTGCCTTTGCCTAGTTTCAGACGCAGGGAC
AGAGCTCATCGGGAAATCAAGGATATTTTCTATAAGGCAATCCAGAAACGCAGACAGTCT
CAAGAAAAAATTGATGACATTCTCCAAACTTTACTAGATGCTACATACAAGGATGGGCGT
CCTTTGACTGATGATGAAGTAGCAGGGATGCTTATTGGATTACTCTTGGCAGGGCAGCAT
ACATCCTCAACTACTAGTGCTTGGATGGGCTTCTTTTTGGCCAGAGACAAAACACTTCAA
AAAAAATGTTATTTAGAACAGAAAACAGTCTGTGGAGAGAATCTGCCTCCTTTAACTTAT
GACCAGCTCAAGGATCTAAATTTACTTGATCGCTGTATAAAAGAAACATTAAGACTTAGA
CCTCCTATAATGATCATGATGAGAATGGCCAGAACTCCTCAGACTGTGGCAGGGTATACC
ATTCCTCCAGGACATCAGGTGTGTGTTTCTCCCACTGTCAATCAAAGACTTAAAGACTCA
TGGGTAGAACGCCTGGACTTTAATCCTGATCGCTACTTACAGGATAACCCAGCATCAGGG
GAAAAGTTTGCCTATGTGCCATTTGGAGCTGGGCGTCATCGTTGTATTGGGGAAAATTTT
GCCTATGTTCAAATTAAGACAATTTGGTCCACTATGCTTCGTTTATATGAATTTGATCTC
ATTGATGGATACTTTCCCACTGTGAATTATACAACTATGATTCACACCCCTGAAAACCCA
GTTATCCGTTACAAACGAAGATCAAAATGA
Enzyme 2 GenBank Gene ID NM_000786 Link Image
Enzyme 2 GeneCard ID CYP51A1 Link Image
Enzyme 2 GenAtlas ID CYP51A1 Link Image
Enzyme 2 HGNC ID HGNC:2649 Link Image
Enzyme 2 Chromosome Location 7
Enzyme 2 Locus 7q21.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Stromstedt M, Rozman D, Waterman MR: The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch Biochem Biophys. 1996 May 1;329(1):73-81. [PubMed Link Image]
  2. Aoyama Y, Noshiro M, Gotoh O, Imaoka S, Funae Y, Kurosawa N, Horiuchi T, Yoshida Y: Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient and conserved P450 species. J Biochem. 1996 May;119(5):926-33. [PubMed Link Image]
  3. Rozman D, Stromstedt M, Waterman MR: The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family. Arch Biochem Biophys. 1996 Sep 15;333(2):466-74. [PubMed Link Image]
  4. Rozman D, Stromstedt M, Tsui LC, Scherer SW, Waterman MR: Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genomics. 1996 Dec 15;38(3):371-81. [PubMed Link Image]
  5. 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]
  6. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  7. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  8. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15218
Enzyme 3 Name Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name CYP51A1
Enzyme 3 Protein Sequence >Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
MAAAAGMLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQL
PAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAA
ALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSI
IEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGF
SHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGR
PLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTY
DQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDS
WVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDL
IDGYFPTVNYTTMIHTPENPVIRYKRRSK
Enzyme 3 Number of Residues 509
Enzyme 3 Molecular Weight 57279
Enzyme 3 Theoretical pI 8.72
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • endopeptidase activity
  • heme binding
  • hydrolase activity
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • peptidase activity
  • serine-type endopeptidase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • cellular protein metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
Enzyme 3 General Function Secondary metabolites biosynthesis, transport and catabolism
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 Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID A4D1F8 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A4D1F8_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID CH236949 Link Image
Enzyme 3 GeneCard ID A4D1F8 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available