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Human Metabolome Database Version 2.5

 

Showing metabocard for Lanosterin (HMDB01251)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:37
Accession Number HMDB01251
Secondary Accession Numbers HMDB01323; HMDB01462
Common Name Lanosterin
Description Lanosterol is a tetracyclic triterpenoid which is the compound from which all steroids are derived. Lanosterol is biochemically synthesized starting from acetyl-CoA by the HMG-CoA reductase pathway. The critical step is the enzymatic conversion of the acyclic terpene squalene to the polycylic lanosterol via 2,3-squalene oxide.(wikipedia)
Synonyms
  1. (3 beta)-Lanosta-8,24-dien-3-ol
  2. (3alpha)-4,4,14-trimethyl-Cholesta-8,24-dien-3-ol
  3. (3beta)-Lanosta-8,24-dien-3-ol
  4. (3beta,5alpha)-4,4,14-trimethyl-Cholesta-8,24-dien-3-ol
  5. 4,4',14alpha-Trimethyl-5alpha-cholesta-8,24-dien-3beta-ol
  6. Botalan base 138
  7. Lanosta-8,24-dien-3-ol
  8. Lanosta-8,24-dien-3beta-ol
  9. Lanosta-8,24-dienol
  10. Lanosterin
  11. Lanosterol
  12. Lanster
Chemical IUPAC Name 4,4,10,13,14-pentamethyl-17-(6-methylhept-5-en-2-yl)-2,3,5,6,7,11,12,15,16,17-decahydro-1H-cyclopenta[a]phenanthren-3-ol
Chemical Formula C30H50O
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 426.717
Monoisotopic Molecular Weight 426.386169
Isomeric SMILES C[C@H](CCC=C(/C)C)[C@H]1CC[C@@]2(C)C3=C(CC[C@]12C)[C@@]1(C)CC[C@H](O)C(C)(C)[C@@H]1CC3
Canonical SMILES CC(CCC=C(C)C)C1CCC2(C)C3=C(CCC12C)C1(C)CCC(O)C(C)(C)C1CC3
KEGG Compound ID C01724 Link Image
BioCyc ID LANOSTEROL Link Image
BiGG ID 38253 Link Image
Wikipedia Link Lanosterol Link Image
NuGOwiki Link HMDB01251 Link Image
Metagene Link HMDB01251 Link Image
METLIN ID 6108 Link Image
PubChem Compound 246983 Link Image
PubChem Substance 4861 Link Image
ChEBI ID 16521 Link Image
CAS Registry Number 79-63-0
InChI Identifier InChI=1/C30H50O/c1-20(2)10-9-11-21(3)22-14-18-30(8)24-12-13-25-27(4,5)26(31)16-17-28(25,6)23(24)15-19-29(22,30)7/h10,21-22,25-26,31H,9,11-19H2,1-8H3/t21-,22-,25+,26+,28-,29-,30+/m1/s1
Synthesis Reference Maienthal, Millard; Franklin, Philip J. Preparation of lanosterol from bromolanosterol. Journal of Organic Chemistry (1955), 20 1627-30.
Melting Point (Experimental) 140.5 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 9.65e-10 mg/mL [MEYLAN,WM et al. (1996)]; 3.76e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 7.72 [Predicted by ALOGPS]; 7.7 [Predicted by PubChem via XLOGP]; 10.79 [MEYLAN,WM & HOWARD,PH (1995)] 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
  • Membrane
  • Cytoplasm
  • endoplasmic reticulum
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. Wikipedia Link Image
Metabolic Enzymes
  1. Cytochrome P450 51A1
  2. Lanosterol synthase
  3. 24-dehydrocholesterol reductase precursor
  4. 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 5497
Enzyme 1 Name Cytochrome P450 51A1
Enzyme 1 Synonyms
  1. CYPLI
  2. P450LI
  3. Sterol 14-alpha demethylase
  4. Lanosterol 14-alpha demethylase
  5. LDM
  6. P450-14DM
  7. P45014DM
Enzyme 1 Gene Name CYP51A1
Enzyme 1 Protein Sequence >Cytochrome P450 51A1 
MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKS
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNS
KNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETK
EYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWL
LPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDE
VAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDL
NLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLD
FNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFP
TVNYTTMIHTPENPVIRYKRRSK
Enzyme 1 Number of Residues 503
Enzyme 1 Molecular Weight 56807
Enzyme 1 Theoretical pI 8.72
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 1 Specific Function Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 3 H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 24-44
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1698396 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16850 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CP51A_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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
ATTGATGGATACTTTCCCACTGTGAATTATACAACTATGATTCACACCCCTGAGAACCCA
GTTATCCGTTACAAACGAAGATCAAAATGA
Enzyme 1 GenBank Gene ID U23942 Link Image
Enzyme 1 GeneCard ID CYP51A1 Link Image
Enzyme 1 GenAtlas ID CYP51A1 Link Image
Enzyme 1 HGNC ID HGNC:2649 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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. 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]
  3. 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]
  4. 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]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5667
Enzyme 2 Name Lanosterol synthase
Enzyme 2 Synonyms
  1. Oxidosqualene--lanosterol cyclase
  2. 2,3-epoxysqualene--lanosterol cyclase
  3. OSC
Enzyme 2 Gene Name LSS
Enzyme 2 Protein Sequence >Lanosterol synthase 
MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDT
KNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLP
AGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNIL
HKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPM
SYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALL
NLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQE
HVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRL
SQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPR
ERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQA
LKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMG
QTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLM
AVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFS
QLYPERALAGHP
Enzyme 2 Number of Residues 732
Enzyme 2 Molecular Weight 83310
Enzyme 2 Theoretical pI 6.60
Enzyme 2 GO Classification
Function
  • catalytic activity
  • lyase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Translation, ribosomal structure and biogenesis
Enzyme 2 Specific Function Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (S)-2,3-epoxysqualene = lanosterol
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 951314 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P48449 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ERG7_HUMAN Link Image
Enzyme 2 PDB ID 1W6J Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >2199 bp 
ATGACGGAGGGCACGTGTCTGCGGCGCCGAGGGGGCCCCTACAAGACCGAGCCCGCCACC
GACCTCGGCCGCTGGCGACTCAACTGCGAGAGGGGCCGGCAGACGTGGACCTACCTGCAG
GACGAGCGCGCCGGCCGCGAGCAGACCGGCCTGGAAGCCTACGCCCTGGGGCTGGACACC
AAGAATTACTTTAAGGACTTGCCCAAAGCCCACACCGCCTTTGAGGGGGCTCTGAACGGG
ATGACATTTTACGTGGGGCTGCAGGCTGAGGATGGGCACTGGACGGGTGATTATGGTGGC
CCACTTTTCCTCCTGCCAGGCCTCCTGATCACTTGCCACGTGGCACGCATCCCTCTGCCA
GCCGGATACAGAGAAGAGATTGTGCGGTACCTGCGGTCAGTGCAGCTCCCTGACGGTGGC
TGGGGCCTGCACATTGAGGATAAGTCCACCGTGTTTGGGACTGCGCTCAACTATGTGTCT
CTCAGAATTCTGGGTGTTGGGCCTGACGATCCTGACCTGGTACGAGCCCGGAACATTCTT
CACAAGAAAGGTGGTGCTGTGGCCATCCCCTCCTGGGGGAAGTTCTGGCTGGCTGTCCTG
AATGTTTACAGCTGGGAAGGCCTCAATACCCTGTTCCCAGAGATGTGGCTGTTTCCTGAC
TGGGCACCGGCACACCCCTCCACACTCTGGTGCCACTGCCGGCAGGTGTACCTGCCCATG
AGCTACTGCTACGCCGTTCGGCTGAGTGCCGCGGAAGACCCGCTGGTCCAGAGCCTCCGC
CAGGAGCTCTATGTGGAGGACTTCGCCAGCATTGACTGGCTGGCGCAGAGGAACAACGTG
GCCCCCGACGAGCTGTACACGCCCCACAGCTGGCTGCTCCGCGTGGTATATGCGCTCCTC
AACCTGTATGAGCACCACCACAGTGCCCACCTGCGGCAGCGGGCCGTGCAGAAGCTGTAT
GAACACATTGTGGCCGACGACCGATTCACCAAGAGCATCAGCATCGGCCCGATCTCGAAA
ACCATCAACATGCTTGTGCGCTGGTATGTGGACGGGCCCGCCTCCACTGCCTTCCAGGAG
CATGTCTCCAGAATCCCGGACTATCTCTGGATGGGCCTTGACGGCATGAAAATGCAGGGC
ACCAACGGCTCACAGATCTGGGACACCGCATTCGCCATCCAGGCTCTGCTTGAGGCGGGC
GGGCACCACAGGCCCGAGTTTTCGTCCTGCCTGCAGAAGGCTCATGAGTTCCTGAGGCTC
TCACAGGTCCCAGATAACCCTCCCGACTACCAGAAGTACTACCGCCAGATGCGCAAGGGT
GGCTTCTCCTTCAGTACGCTGGACTGCGGCTGGATCGTTTCTGACTGCACGGCTGAGGCC
TTGAAGGCTGTGCTGCTCCTGCAGGAGAAGTGTCCCCATGTCACCGAGCACATCCCCAGA
GAACGGCTCTGCGATGCTGTGGCTGTGCTGCTGAACATGAGAAATCCAGATGGAGGGTTC
GCCACCTATGAGACCAAGCGTGGGGGGCACTTGCTGGAGCTGCTGAACCCCTCGGAGGTC
TTCGGGGACATCATGATTGACTACACCTATGTGGAGTGCACCTCAGCCGTGATGCAGGCG
CTTAAGTATTTCCACAAGCGTTTCCCGGAGCACAGGGCAGCGGAGATCCGGGAGACCCTC
ACGCAGGGCTTAGAGTTCTGTCGGCGGCAGCAGAGGGCCGATGGCTCCTGGGAAGGCTCC
TGGGGAGTTTGCTTCACCTACGGCACCTGGTTTGGCCTGGAGGCCTTCGCCTGTATGGGG
CAGACCTACCGAGATGGGACTGCCTGTGCAGAGGTCTCCCGGGCCTGTGACTTCCTGCTG
TCCCGGCAGATGGCAGACGGAGGCTGGGGGGAGGACTTTGAGTCCTGCGAGGAGCGGCGT
TATTTGCAGAGTGCCCAGTCCCAGATCCATAACACATGCTGGGCCATGATGGGGCTGATG
GCCGTTCGGCATCCTGACATCGAGGCCCAGGAGAGAGGAGTCCGGTGTCTACTTGAGAAA
CAGCTCCCCAATGGCGACTGGCCGCAGGAAAACATTGCTGGGGTCTTCAACAAGTCCTGT
GCCATCTCCTACACGAGCTACAGGAACATCTTCCCCATCTGGGCCCTCGGCCGCTTCTCC
CAGCTGTACCCTGAGAGAGCCCTTGCTGGCCACCCCTGA
Enzyme 2 GenBank Gene ID U22526 Link Image
Enzyme 2 GeneCard ID LSS Link Image
Enzyme 2 GenAtlas ID LSS Link Image
Enzyme 2 HGNC ID HGNC:6708 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Baker CH, Matsuda SP, Liu DR, Corey EJ: Molecular cloning of the human gene encoding lanosterol synthase from a liver cDNA library. Biochem Biophys Res Commun. 1995 Aug 4;213(1):154-60. [PubMed Link Image]
  2. Sung CK, Shibuya M, Sankawa U, Ebizuka Y: Molecular cloning of cDNA encoding human lanosterol synthase. Biol Pharm Bull. 1995 Oct;18(10):1459-61. [PubMed Link Image]
  3. Roessler E, Mittaz L, Du Y, Scott HS, Chang J, Rossier C, Guipponi M, Matsuda SP, Muenke M, Antonarakis SE: Structure of the human Lanosterol synthase gene and its analysis as a candidate for holoprosencephaly (HPE1). Hum Genet. 1999 Nov;105(5):489-95. [PubMed Link Image]
  4. Young M, Chen H, Lalioti MD, Antonarakis SE: The human lanosterol synthase gene maps to chromosome 21q22.3. Hum Genet. 1996 May;97(5):620-4. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 7345
Enzyme 3 Name 24-dehydrocholesterol reductase precursor
Enzyme 3 Synonyms
  1. 3-beta- hydroxysterol delta-24-reductase
  2. Seladin-1
  3. Diminuto/dwarf1 homolog
Enzyme 3 Gene Name DHCR24
Enzyme 3 Protein Sequence >24-dehydrocholesterol reductase precursor 
MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKL
SSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMD
ILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKY
GLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKL
RFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYY
KPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVP
PKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQ
PGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREE
FWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH
Enzyme 3 Number of Residues 516
Enzyme 3 Molecular Weight 60102
Enzyme 3 Theoretical pI 8.24
Enzyme 3 GO Classification
Function
—
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Energy production and conversion
Enzyme 3 Specific Function Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-22
Enzyme 3 Transmembrane Regions
  • 32-52
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 10442025 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q15392 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name DHC24_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1551 bp 
ATGGAGCCCGCCGTGTCGCTGGCCGTGTGCGCGCTGCTCTTCCTGCTGTGGGTGCGCCTG
AAGGGGCTGGAGTTCGTGCTCATCCACCAGCGCTGGGTGTTCGTGTGCCTCTTCCTCCTG
CCGCTCTCGCTTATCTTCGATATCTACTACTACGTGCGCGCCTGGGTGGTGTTCAAGCTC
AGCAGCGCTCCGCGCCTGCACGAGCAGCGCGTGCGGGACATCCAGAAGCAGGTGCGGGAA
TGGAAGGAGCAGGGTAGCAAGACCTTCATGTGCACGGGGCGCCCTGGCTGGCTCACTGTC
TCACTACGTGTCGGGAAGTACAAGAAGACACACAAAAACATCATGATCAACCTGATGGAC
ATTCTGGAAGTGGACACCAAGAAACAGATTGTCCGTGTGGAGCCCTTGGTGACCATGGGC
CAGGTGACTGCCCTGCTGACCTCCATTGGCTGGACTCTCCCCGTGTTGCCTGAGCTTGAT
GACCTCACAGTGGGGGGCTTGATCATGGGCACAGGCATCGAGTCATCATCCCACAAGTAC
GGCCTGTTCCAACACATCTGCACTGCTTACGAGCTGGTCCTGGCTGATGGCAGCTTTGTG
CGATGCACTCCGTCCGAAAACTCAGACCTGTTCTATGCCGTACCCTGGTCCTGTGGGACG
CTGGGTTTCCTGGTGGCCGCTGAGATCCGCATCATCCCTGCCAAGAAGTACGTCAAGCTG
CGTTTCGAGCCAGTGCGGGGCCTGGAGGCTATCTGTGCCAAGTTCACCCACGAGTCCCAG
CGGCAGGAGAACCACTTCGTGGAAGGGCTGCTCTACTCCCTGGATGAGGCTGTCATTATG
ACAGGGGTCATGACAGATGAGGCAGAGCCCAGCAAGCTGAATAGCATTGGCAATTACTAC
AAGCCGTGGTTCTTTAAGCATGTGGAGAACTATCTGAAGACAAACCGAGAGGGCCTGGAG
TACATTCCCTTGAGACACTACTACCACCGCCACACGCGCAGCATCTTCTGGGAGCTCCAG
GACATCATCCCCTTTGGCAACAACCCCATCTTCCGCTACCTCTTTGGCTGGATGGTGCCT
CCCAAGATCTCCCTCCTGAAGCTGACCCAGGGTGAGACCCTGCGCAAGCTGTACGAGCAG
CACCACGTGGTGCAGGACATGCTGGTGCCCATGAAGTGCCTGCAGCAGGCCCTGCACACC
TTCCAAAACGACATCCACGTCTACCCCATCTGGCTGTGTCCGTTCATCCTGCCCAGCCAG
CCAGGCCTAGTGCACCCCAAAGGAAATGAGGCAGAGCTCTACATCGACATTGGAGCATAT
GGGGAGCCGCGTGTGAAACACTTTGAAGCCAGGTCCTGCATGAGGCAGCTGGAGAAGTTT
GTCCGCAGCGTGCATGGCTTCCAGATGCTGTATGCCGACTGCTACATGAACCGGGAGGAG
TTCTGGGAGATGTTTGATGGCTCCTTGTACCACAAGCTGCGAGAGAAGCTGGGTTGCCAG
GACGCCTTCCCCGAGGTGTACGACAAGATCTGCAAGGCCGCCAGGCACTGA
Enzyme 3 GenBank Gene ID AF261758 Link Image
Enzyme 3 GeneCard ID DHCR24 Link Image
Enzyme 3 GenAtlas ID DHCR24 Link Image
Enzyme 3 HGNC ID HGNC:2859 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p33-p31.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Greeve I, Hermans-Borgmeyer I, Brellinger C, Kasper D, Gomez-Isla T, Behl C, Levkau B, Nitsch RM: The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress. J Neurosci. 2000 Oct 1;20(19):7345-52. [PubMed Link Image]
  2. Waterham HR, Koster J, Romeijn GJ, Hennekam RC, Vreken P, Andersson HC, FitzPatrick DR, Kelley RI, Wanders RJ: Mutations in the 3beta-hydroxysterol Delta24-reductase gene cause desmosterolosis, an autosomal recessive disorder of cholesterol biosynthesis. Am J Hum Genet. 2001 Oct;69(4):685-94. Epub 2001 Aug 22. [PubMed Link Image]
  3. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15218
Enzyme 4 Name Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name CYP51A1
Enzyme 4 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 4 Number of Residues 509
Enzyme 4 Molecular Weight 57279
Enzyme 4 Theoretical pI 8.72
Enzyme 4 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 4 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID A4D1F8 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A4D1F8_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID CH236949 Link Image
Enzyme 4 GeneCard ID A4D1F8 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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 4 Metabolite References Not Available