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Human Metabolome Database Version 2.5

 

Showing metabocard for 7-Dehydrocholesterol (HMDB00032)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:57:38
Accession Number HMDB00032
Secondary Accession Numbers Not Available
Common Name 7-Dehydrocholesterol
Description 7-Dehydrocholesterol is a zoosterol (a sterol produced by animals rather than plants). It is a provitamin-D. The presence of this compound in skin enables humans to manufacture vitamin D3 from ultra-violet rays in the sun light, via an intermediate isomer provitamin D3. It is also found in breast milk.
Synonyms
  1. (-)-7-dehydrocholesterol
  2. (3b)-Cholesta-5,7-dien-3-ol
  3. (3beta)-Cholesta-5,7-dien-3-ol
  4. 10,13-dimethyl-17-(6-methylheptan-2-yl)-2,3,4,9,11,12,14,15,16,17-decahydro-1H-cyclopenta[a]phenanthren-3-ol
  5. 17-(1,5-dimethylhexyl)-10,13-dimethyl-2,3,4,9,10,11,12,13,14,15,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-3-ol
  6. 5,7-Cholestadien-3-beta-ol
  7. 5,7-Cholestandien-3-ol
  8. 5,7-Cholestandien-3beta-ol
  9. 7,8-Didehydrocholesterol
  10. 7,8-dehydro-cholesterol
  11. 7-Dehydrocholesterin
  12. 7-Dehydrocholesterol
  13. 7-dehydro-cholesterol
  14. 7DHC
  15. Cholesta-5,7-dien-3-beta-ol
  16. Cholesta-5,7-dien-3-ol
  17. Cholesta-5,7-dien-3beta-ol
  18. Dehydrocholesterin
  19. Dehydrocholesterol
  20. Provitamin D3
  21. cholesta-5,7-dien-3 beta -ol
  22. cholesta-5,7-dien-3b-ol
  23. delta5,7-Cholestadien-3beta-ol
  24. delta5,7-Cholesterol
  25. delta7-Cholesterol
  26. provitamin-D3
Chemical IUPAC Name 10,13-dimethyl-17-(6-methylheptan-2-yl)-2,3,4,9,11,12,14,15,16,17-decahydro-1H-cyclopenta[a]phenanthren-3-ol
Chemical Formula C27H44O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Vitamin D3 derivatives
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • alkene
Biofunction
  • Hormones, Membrane component
Application
—
Source
  • Endogenous
Average Molecular Weight 384.638
Monoisotopic Molecular Weight 384.339203
Isomeric SMILES CC(C)CCC[C@@H](C)[C@H]1CC[C@H]2C3=CC=C4C[C@@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(C)CCCC(C)C1CCC2C3=CC=C4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID C01164 Link Image
BioCyc ID 7-DEHYDRO-CHOLESTEROL Link Image
BiGG ID 36958 Link Image
Wikipedia Link 7-Dehydrocholesterol Link Image
NuGOwiki Link HMDB00032 Link Image
Metagene Link HMDB00032 Link Image
METLIN ID 5101 Link Image
PubChem Compound 439423 Link Image
PubChem Substance 3132652 Link Image
ChEBI ID 17759 Link Image
CAS Registry Number 434-16-2
InChI Identifier InChI=1/C27H44O/c1-18(2)7-6-8-19(3)23-11-12-24-22-10-9-20-17-21(28)13-15-26(20,4)25(22)14-16-27(23,24)5/h9-10,18-19,21,23-25,28H,6-8,11-17H2,1-5H3/t19-,21+,23-,24+,25+,26+,27-/m1/s1
Synthesis Reference William G. Dauben, Jerome F. Eastham, and Robert A. Micheli A new method for the preparation of 7-dehydrocholesterol. Journal of the American Chemical Society (1951), 73 4496.
Melting Point (Experimental) 150.5 oC
Experimental Water Solubility 1 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 1.08e-07 mg/mL [MEYLAN,WM et al. (1996)]; 1.48e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 7.30 [Predicted by ALOGPS]; 7.2 [Predicted by PubChem via XLOGP]; 8.65 [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 Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Adrenal Gland —
Brain —
Fetus —
Fibroblasts —
Liver —
Skin —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 5.0 +/- 2.2 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Johnson DW, ten Brink HJ, Jakobs C: A rapid screening procedure for cholesterol and dehydrocholesterol by electrospray ionization tandem mass spectrometry. J Lipid Res. 2001 Oct;42(10):1699-705. [PubMed Link Image]
Biofluid CSF
Value 0 - 0.02 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Jira PE, Wevers RA, de Jong J, Rubio-Gozalbo E, Janssen-Zijlstra FS, van Heyst AF, Sengers RC, Smeitink JA: Simvastatin. A new therapeutic approach for Smith-Lemli-Opitz syndrome. J Lipid Res. 2000 Aug;41(8):1339-46. [PubMed Link Image]
Biofluid Urine
Value 0.029 (0.0068-0.051) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Jezela-Stanek A, Malunowicz EM, Ciara E, Popowska E, Goryluk-Kozakiewicz B, Spodar K, Czerwiecka M, Jezuita J, Nowaczyk MJ, Krajewska-Walasek M: Maternal urinary steroid profiles in prenatal diagnosis of Smith-Lemli-Opitz syndrome: first patient series comparing biochemical and molecular studies. Clin Genet. 2006 Jan;69(1):77-85. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 369.0 (46.0 - 1220.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Smith-Lemli-Opitz syndrome
Comments Not Available
References
  • Johnson DW, ten Brink HJ, Jakobs C: A rapid screening procedure for cholesterol and dehydrocholesterol by electrospray ionization tandem mass spectrometry. J Lipid Res. 2001 Oct;42(10):1699-705. [PubMed Link Image]
Biofluid CSF
Value 0.3 +/- 0.2 (0.1 - 0.6) uM
Age Infant:0-1 yr old
Sex Both
Condition Smith-Lemli-Opitz syndrome
Comments Not Available
References
  • van Rooij A, Nijenhuis AA, Wijburg FA, Schutgens RB: Highly increased CSF concentrations of cholesterol precursors in Smith-Lemli-Opitz syndrome. J Inherit Metab Dis. 1997 Aug;20(4):578-80. [PubMed Link Image]
Associated Disorders
Condition References
Smith-Lemli-Opitz syndrome
OMIM ID
  • 270400 Link Image (Smith-Lemli-Opitz syndrome)
Pathways
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Lehmann B, Genehr T, Knuschke P, Pietzsch J, Meurer M: UVB-induced conversion of 7-dehydrocholesterol to 1alpha,25-dihydroxyvitamin D3 in an in vitro human skin equivalent model. J Invest Dermatol. 2001 Nov;117(5):1179-85. [PubMed Link Image]
  2. Muzzin KB, Harper LF: Smith-Lemli-Opitz syndrome: a review, case report and dental implications. Spec Care Dentist. 2003;23(1):22-7. [PubMed Link Image]
  3. Paterson CR, Moody JP, Pennington CR: Skin content of 7-dehydrocholesterol in patients with malabsorption. Nutrition. 1997 Sep;13(9):771-3. [PubMed Link Image]
  4. Jira PE, Wevers RA, de Jong J, Rubio-Gozalbo E, Janssen-Zijlstra FS, van Heyst AF, Sengers RC, Smeitink JA: Simvastatin. A new therapeutic approach for Smith-Lemli-Opitz syndrome. J Lipid Res. 2000 Aug;41(8):1339-46. [PubMed Link Image]
  5. Johnson DW, ten Brink HJ, Jakobs C: A rapid screening procedure for cholesterol and dehydrocholesterol by electrospray ionization tandem mass spectrometry. J Lipid Res. 2001 Oct;42(10):1699-705. [PubMed Link Image]
  6. van Rooij A, Nijenhuis AA, Wijburg FA, Schutgens RB: Highly increased CSF concentrations of cholesterol precursors in Smith-Lemli-Opitz syndrome. J Inherit Metab Dis. 1997 Aug;20(4):578-80. [PubMed Link Image]
  7. Andersson HC, Frentz J, Martinez JE, Tuck-Muller CM, Bellizaire J: Adrenal insufficiency in Smith-Lemli-Opitz syndrome. Am J Med Genet. 1999 Feb 19;82(5):382-4. [PubMed Link Image]
  8. GarciaFuentes E, icioso Recio MV, del Castillo Acedo Del Olmo E, atas Jurado MM, Arana Aguera M, Lopez Lopez J: [Biochemical diagnosis of Smith-Lemli-Opitz syndrome in a patient with congenital adrenal hyperplasia] An Esp Pediatr. 2000 Nov;53(5):482-7. [PubMed Link Image]
  9. Jezela-Stanek A, Malunowicz EM, Ciara E, Popowska E, Goryluk-Kozakiewicz B, Spodar K, Czerwiecka M, Jezuita J, Nowaczyk MJ, Krajewska-Walasek M: Maternal urinary steroid profiles in prenatal diagnosis of Smith-Lemli-Opitz syndrome: first patient series comparing biochemical and molecular studies. Clin Genet. 2006 Jan;69(1):77-85. [PubMed Link Image]
  10. Moody JP, Humphries CA, Allan SM, Paterson CR: Determination of 7-dehydrocholesterol in human skin by high-performance liquid chromatography. J Chromatogr. 1990 Aug 24;530(1):19-27. [PubMed Link Image]
  11. Wikipedia Link Image
Metabolic Enzymes
  1. Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
  2. Lathosterol oxidase
  3. Nonspecific lipid-transfer protein
  4. 7-dehydrocholesterol reductase
  5. Cytochrome P450 11A1, mitochondrial precursor
  6. 24-dehydrocholesterol reductase precursor
Enzyme 1 [top]
Enzyme 1 ID 5269
Enzyme 1 Name Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
Enzyme 1 Synonyms
  1. HMG-CoA synthase
  2. 3-hydroxy-3-methylglutaryl coenzyme A synthase
Enzyme 1 Gene Name HMGCS2
Enzyme 1 Protein Sequence >Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor 
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALE
VYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLP
WDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWM
ESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYD
FYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIF
HTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKAS
QDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASF
FSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPG
DTNSLFPGTWYLERVDEQHRRKYARRPV
Enzyme 1 Number of Residues 508
Enzyme 1 Molecular Weight 56636
Enzyme 1 Theoretical pI 8.28
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydroxymethylglutaryl-CoA synthase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • acetyl-CoA metabolism
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase
Enzyme 1 Pathways
  • Butyrate Metabolism (map00650 Link Image)
  • Synthesis and Degradation of Ketone Bodies (map00072 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 1 Reactions
  • acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-17
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 619877 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P54868 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name HMCS2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1527 bp 
ATGCAGCGTCTGTTGACTCCAGTGAAGCGCATTCTGCAACTGACAAGAGCGGTGCAGGAA
ACCTCCCTCACACCTGCTCGCCTGCTCCCAGTAGCCCACCAAAGGTTTTCTACAGCCTCT
GCTGTCCCCCTGGCCAAAACAGATACTTGGCCAAAGGACGTGGGCATCCTGGCCCTGGAG
GTCTACTTCCCAGCCCAATATGTGGACCAAACTGACCTGGAGAAGTATAACAATGTGGAA
GCAGGAAAGTATACAGTGGGCTTGGGCCAGACCCGTATGGGCTTCTGCTCAGTCCAAGAG
GACATCAACTCCCTGTGCCTGACGGTGGTGCAACGGCTGATGGAGCGCATACAGCTCCCA
TGGGACTCTGTGGGCAGGCTGGAAGTAGGCACTGAGACCATCATTGACAAGTCCAAAGCT
GTCAAAACAGTGCTCATGGAACTCTTCCAGGATTCAGGCAATACTGATATTGAGGGCATA
GATACCACCAATGCCTGCTACGGTGGTACTGCCTCCCTCTTCAATGCTGCCAACTGGATG
GAGTCCAGTTCCTGGGATGGTCGTTATGCCATGGTGGTCTGTGGAGACATTGCCGTCTAT
CCCAGTGGTAATGCTCGTCCCACAGGTGGGGCCGGAGCTGTGGCTATGCTGATTGGCCCA
AAGGCCCCTCTGGCCCTGGAGCGAGGGCTGAGGGGAACCCATATGGAGAATGTGTATGAC
TTCTACAAACCAAATTTGGCCTCGGAGTACCCAATAGTGGATGGGAAGCTTTCCATCCAG
TGCTACTTGCGGGCCTTGGATCGATGTTACACATCATACCGTAAAAAAATCCAGAATCAG
TGGAAGCAAGCTGGCAGCGATCGACCCTTCACCCTTGACGATTTACAGTATATGATCTTT
CATACACCCTTTTGCAAGATGGTCCAGAAGTCTCTGGCTCGCCTGATGTTCAATGACTTC
CTGTCAGCCAGCAGTGACACACAAACCAGCTTATATAAGGGGCTGGAGGCTTTCGGGGGG
CTAAAGCTGGAAGACACCTACACCAACAAGGACCTGGATAAAGCACTTCTAAAGGCCTCT
CAGGACATGTTCGACAAGAAAACCAAGGCTTCCCTTTACCTCTCCACTCACAATGGGAAC
ATGTACACCTCATCCCTGTACGGGTGCCTGGCCTCGCTTCTGTCCCACCACTCTGCCCAA
GAACTGGCTGGCTCCAGGATTGGTGCCTTCTCTTATGGCTCTGGTTTAGCAGCAAGTTTC
TTTTCATTTCGAGTATCCCAGGATGCTGCTCCAGGCTCTCCCCTGGACAAGTTGGTGTCC
AGCACATCAGACCTGCCAAAACGCCTAGCCTCCCGAAAGTGTGTGTCTCCTGAGGAGTTC
ACAGAAATAATGAACCAAAGAGAGCAATTCTACCATAAGGTGAATTTCTCCCCACCTGGT
GACACAAACAGCCTTTTCCCAGGTACTTGGTACCTGGAGCGAGTGGACGAGCAGCATCGC
CGAAAGTATGCCCGGCGTCCCGTCTAA
Enzyme 1 GenBank Gene ID X83618 Link Image
Enzyme 1 GeneCard ID HMGCS2 Link Image
Enzyme 1 GenAtlas ID HMGCS2 Link Image
Enzyme 1 HGNC ID HGNC:5008 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p13-p12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Mascaro C, Buesa C, Ortiz JA, Haro D, Hegardt FG: Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. Arch Biochem Biophys. 1995 Mar 10;317(2):385-90. [PubMed Link Image]
  2. Boukaftane Y, Mitchell GA: Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene. Gene. 1997 Aug 22;195(2):121-6. [PubMed Link Image]
  3. Boukaftane Y, Duncan A, Wang S, Labuda D, Robert MF, Sarrazin J, Schappert K, Mitchell GA: Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution. Genomics. 1994 Oct;23(3):552-9. [PubMed Link Image]
Enzyme 1 Metabolite References
  1. Honda M, Tint GS, Honda A, Nguyen LB, Chen TS, Shefer S: 7-Dehydrocholesterol down-regulates cholesterol biosynthesis in cultured Smith-Lemli-Opitz syndrome skin fibroblasts. J Lipid Res. 1998 Mar;39(3):647-57. [PubMed Link Image]
Enzyme 2 [top]
Enzyme 2 ID 5367
Enzyme 2 Name Lathosterol oxidase
Enzyme 2 Synonyms
  1. Lathosterol 5-desaturase
  2. Delta(7-sterol 5-desaturase
  3. C-5 sterol desaturase
  4. Sterol-C5- desaturase
Enzyme 2 Gene Name SC5DL
Enzyme 2 Protein Sequence >Lathosterol oxidase 
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
Enzyme 2 Number of Residues 299
Enzyme 2 Molecular Weight 35301
Enzyme 2 Theoretical pI 8.24
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 32-52 79-99 117-137 186-206
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1906796 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O75845 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SC5D_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >711 bp 
ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTAAGAATGAAAAATTAT
TCAATGGAGAGTTTACAAAGACTGAATAGATTATTGCCCAGTTATTCTTAA
Enzyme 2 GenBank Gene ID D85181 Link Image
Enzyme 2 GeneCard ID SC5DL Link Image
Enzyme 2 GenAtlas ID SC5DL Link Image
Enzyme 2 HGNC ID HGNC:10547 Link Image
Enzyme 2 Chromosome Location 11
Enzyme 2 Locus 11q23.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed Link Image]
  2. Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed Link Image]
  3. Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed Link Image]
  4. Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed Link Image]
  5. Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed Link Image]
Enzyme 2 Metabolite References
  1. Sugawara T, Fujimoto Y, Ishibashi T: Molecular cloning and structural analysis of human sterol C5 desaturase. Biochim Biophys Acta. 2001 Oct 31;1533(3):277-84. [PubMed Link Image]
Enzyme 3 [top]
Enzyme 3 ID 5678
Enzyme 3 Name Nonspecific lipid-transfer protein
Enzyme 3 Synonyms
  1. Propanoyl-CoA C- acyltransferase
  2. NSL-TP
  3. Sterol carrier protein 2
  4. SCP-2
  5. Sterol carrier protein X
  6. SCP-X
  7. SCP-chi
  8. SCPX
Enzyme 3 Gene Name SCP2
Enzyme 3 Protein Sequence >Nonspecific lipid-transfer protein 
MSSSPWEPATLRRVFVVGVGMTKFVKPGAENSRDYPDLAEEAGKKALADAQIPYSAVDQA
CVGYVFGDSTCGQRAIYHSLGMTGIPIINVNNNCATGSTALFMARQLIQGGVAECVLALG
FEKMSKGSLGIKFSDRTIPTDKHVDLLINKYGLSAHPVAPQMFGYAGKEHMEKYGTKIEH
FAKIGWKNHKHSVNNPYSQFQDEYSLDEVMASKEVFDFLTILQCCPTSDGAAAAILASEA
FVQKYGLQSKAVEILAQEMMTDLPSSFEEKSIIKMVGFDMSKEAARKCYEKSGLTPNDID
VIELHDCFSTNELLTYEALGLCPEGQGATLVDRGDNTYGGKWVINPSGGLISKGHPLGAT
GLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGIGGAVVVTLYKMGFPEAASSFRTHQIE
AVPTSSASDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKN
GKGSVLPNSDKKADCTITMADSDFLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQL
QPGNAKL
Enzyme 3 Number of Residues 547
Enzyme 3 Molecular Weight 58994
Enzyme 3 Theoretical pI 6.88
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
  • steroid binding
  • sterol carrier activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis
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 1773239 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22307 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NLTP_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1644 bp 
ATGTCCTCTTCCCCGTGGGAGCCTGCAGCCCTGCGCCGGGTGTTCGTGGTGGGGGTTGGC
ATGACCAAGTTTGTGAAGCCTGGAGCTGAGAATTCAAGAGACTACCCTGACTTGGCAGAA
GAAGCAGGCAAGAAGGCTTTAGCTGATGCACAGATCCCTTATTCAGCAGTGGACCAGGCA
TGTGTTGGCTATGTTTTTGGTGACTCTACCTGTGGGCAGAGGGCTATCTATCACAGTTTG
GGAATGACTGGAATTCCTATAATCAATGTCAACAATAACTGTGCTACTGGTTCTACTGCT
TTGTTTATGGCCCGCCAGCTGATTCAGGGTGGTGTGGCAGAATGTGTCTTGGCTCTTGGG
TTTGAGAAGATGAGTAAGGGAAGCCTTGGAATAAAATTTTCAGATAGAACCATTCCCACT
GATAAGCATGTTGACCTCCTGATCAATAAGTATGGATTGTCTGCTCACCCAGTTGCTCCT
CAGATGTTTGGGTATGCTGGAAAAGAACATATGGAAAAATATGGAACAAAAATTGAACAC
TTTGCAAAAATTGGATGGAAAAATCATAAACATTCAGTTAATAACCCGTATTCCCAGTTC
CAAGATGAATACAGTTTAGATGAAGTGATGGCATCTAAAGAAGTTTTTGATTTTTTGACT
ATCTTACAATGTTGTCCCACTTCAGATGGTGCTGCAGCAGCAATTTTGGCCAGTGAAGCA
TTTGTACAGAAGTATGGCCTGCAATCCAAAGCTGTGGAAATTTTGGCACAAGAAATGATG
ACTGATTTGCCAAGCTCGTTTGAAGAAAAAAGCATTATTAAAATGGTTGGCTTTGATATG
AGTAAAGAAGCTGCAAGAAAATGCTATGAGAAATCTGGCCTTACACCAAATGATATTGAC
GTAATAGAACTTCACGATTGCTTTTCTACCAACGAACTCCTGACTTATGAAGCACTCGGA
CTCTGTCCAGAAGGACAAGGTGCAACGCTGGTTGATAGAGGAGATAATACATATGGAGGA
AAGTGGGTCATAAATCCTAGTGGTGGACTGATTTCAAAGGGACACCCACTAGGCGCTACA
GGTCTTGCTCAGTGTGCAGAACTCTGCTGGCAGCTGAGAGGGGAAGCCGGAAAGAGGCAA
GTTCCTGGTGCAAAGGTGGCTCTGCAGCATAATTTAGACATTGGAGGAGCTGTGGTTGTA
ACACTCTACAAGATGGGTTTTCCGGAAGCCGCCAGTTCTTTTAGAACTCATCAAATTGAA
GCTGTTCCAACCAGCTCTGCAAGTGATGGATTTAAGGCAAATCTTGTTTTTAAGGAGATT
GAGAAGAAACTTGAAGAGGAAGGGGAACAGTTTGTGAAGAAAATCGGTGGTATTTTTGCC
TTCAAGGTGAAAGATGGCCCTGGGGGTAAAGAGGCCACCTGGGTGGTGGATGTGAAGAAT
GGCAAAGGATCAGTGCTTCCTAACTCAGATAAGAAGGCTGACTGCACAATCACAATGGCT
GACTCAGACTTCCTGGCTTTAATGACTGGTAAAATGAATCCTCAGTCGGCCTTCTTTCAA
GGCAAATTGAAAATCACTGGCAACATGGGTCTCGCTATGAAGTTACAAAATCTTCAGCTT
CAGCCAGGCAACGCTAAGCTCTGA
Enzyme 3 GenBank Gene ID U11313 Link Image
Enzyme 3 GeneCard ID SCP2 Link Image
Enzyme 3 GenAtlas ID SCP2 Link Image
Enzyme 3 HGNC ID HGNC:10606 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p32
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ohba T, Rennert H, Pfeifer SM, He Z, Yamamoto R, Holt JA, Billheimer JT, Strauss JF 3rd: The structure of the human sterol carrier protein X/sterol carrier protein 2 gene (SCP2). Genomics. 1994 Nov 15;24(2):370-4. [PubMed Link Image]
  2. He Z, Yamamoto R, Furth EE, Schantz LJ, Naylor SL, George H, Billheimer JT, Strauss JF 3rd: cDNAs encoding members of a family of proteins related to human sterol carrier protein 2 and assignment of the gene to human chromosome 1 p21----pter. DNA Cell Biol. 1991 Oct;10(8):559-69. [PubMed Link Image]
  3. Yamamoto R, Kallen CB, Babalola GO, Rennert H, Billheimer JT, Strauss JF 3rd: Cloning and expression of a cDNA encoding human sterol carrier protein 2. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):463-7. [PubMed Link Image]
  4. Yamamoto R: [Localization of human sterol carrier protein 2 gene and cDNA expression in COS-7 cell] Hokkaido Igaku Zasshi. 1992 Nov;67(6):839-48. [PubMed Link Image]
  5. Szyperski T, Scheek S, Johansson J, Assmann G, Seedorf U, Wuthrich K: NMR determination of the secondary structure and the three-dimensional polypeptide backbone fold of the human sterol carrier protein 2. FEBS Lett. 1993 Nov 29;335(1):18-26. [PubMed Link Image]
Enzyme 3 Metabolite References
  1. Morin RJ, Brun MJ, Srikantaiah MV: Effect of age and cholestyramine feeding on rat liver 3-hydroxy-3-methyl glutaryl CoA reductase, sterol carrier protein 1 and sterol carrier protein 2 activities. Lipids. 1982 Jul;17(7):507-10. [PubMed Link Image]
Enzyme 4 [top]
Enzyme 4 ID 5819
Enzyme 4 Name 7-dehydrocholesterol reductase
Enzyme 4 Synonyms
  1. 7-DHC reductase
  2. Sterol Delta(7-reductase
  3. Putative sterol reductase SR-2
Enzyme 4 Gene Name DHCR7
Enzyme 4 Protein Sequence >7-dehydrocholesterol reductase 
MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMA
CDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHK
FLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPL
LWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFN
GRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHD
HFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDL
FRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCL
ACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF
Enzyme 4 Number of Residues 475
Enzyme 4 Molecular Weight 54490
Enzyme 4 Theoretical pI 8.82
Enzyme 4 GO Classification
Function
—
Process
—
Component
  • cell
  • membrane
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Production of cholesterol by reduction of C7-C8 double bond of 7-dehydrocholesterol (7-DHC)
Enzyme 4 Pathways
Enzyme 4 Reactions
  • cholesterol + NADP+ = cholesta-5,7-dien-3beta-ol + NADPH + H+
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 40-60 154-174 177-197 266-286 306-326 331-351 420-440
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 4191398 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9UBM7 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DHCR7_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1428 bp 
ATGGCTGCAAAATCGCAACCCAACATTCCCAAAGCCAAGAGTCTAGATGGCGTCACCAAT
GACAGAACCGCATCTCAAGGGCAGTGGGGCCGTGCCTGGGAGGTGGACTGGTTTTCACTG
GCGAGCGTCATCTTCCTACTGCTGTTCGCCCCCTTCATCGTCTACTACTTCATCATGGCT
TGTGACCAATACAGCTGCGCCCTGACCGGCCCTGTGGTGGACATCGTCACCGGACATGCT
CGGCTCTCGGACATCTGGGCCAAGACTCCACCTATAACGAGGAAAGCCGCCCAGCTCTAT
ACCTTGTGGGTCACCTTCCAGGTGCTTCTGTACACGTCTCTCCCTGACTTCTGCCATAAG
TTTCTACCCGGCTACGTAGGAGGCATCCAGGAGGGGGCCGTGACTCCTGCAGGGGTTGTG
AACAAGTATCAGATCAACGGCCTGCAAGCCTGGCTCCTCACGCACCTGCTCTGGTTTGCA
AACGCTCATCTCCTGTCCTGGTTCTCGCCCACCATCATCTTCGACAACTGGATCCCACTG
CTGTGGTGCGCCAACATCCTTGGCTATGCCGTCTCCACCTTCGCCATGGTCAAGGGCTAC
TTCTTCCCCACCAGCGCCAGAGACTGCAAATTCACAGGCAATTTCTTTTACAACTACATG
ATGGGCATCGAGTTTAACCCTCGGATCGGGAAGTGGTTTGACTTCAAGCTGTTCTTCAAT
GGGCGCCCCGGGATCGTCGCCTGGACCCTCATCAACCTGTCCTTCGCAGCGAAGCAGCGG
GAGCTCCACAGCCATGTGACCAATGCCATGGTCCTGGTCAACGTCCTGCAGGCCATCTAC
GTGATTGACTTCTTCTGGAACGAAACCTGGTACCTGAAGACCATTGACATCTGCCATGAC
CACTTCGGGTGGTACCTGGGCTGGGGCGACTGTGTCTGGCTGCCTTATCTTTACACGCTG
CAGGGTCTGTACTTGGTGTACCACCCCGTGCAGCTGTCCACCCCGCACGCCGTGGGCGTC
CTGCTGCTGGGCCTGGTGGGCTACTACATCTTCCGGGTGGCCAACCACCAGAAGGACCTG
TTCCGCCGCACGGATGGGCGCTGCCTCATCTGGGGCAGGAAGCCCAAGGTCATCGAGTGC
TCCTACACATCCGCCGACGGGCAGAGGCACCACAGCAAGCTGCTGGTGTCGGGCTTCTGG
GGCGTGGCCCGCCACTTCAACTACGTCGGCGACCTGATGGGCAGCCTGGCCTACTGCCTG
GCCTGTGGCGGTGGCCACCTGCTGCCCTACTTCTACATCATCTACATGGCCATCCTGCTG
ACCCACCGCTGCCTCCGGGACGAGCACCGCTGCGCCAGCAAGTACGGCCGGGACTGGGAG
CGCTACACCGCCGCAGTGCCTTACCGCCTGCTGCCTGGAATCTTCTAA
Enzyme 4 GenBank Gene ID AF096305 Link Image
Enzyme 4 GeneCard ID DHCR7 Link Image
Enzyme 4 GenAtlas ID DHCR7 Link Image
Enzyme 4 HGNC ID HGNC:2860 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q13.2-q13.5
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Waterham HR, Wijburg FA, Hennekam RC, Vreken P, Poll-The BT, Dorland L, Duran M, Jira PE, Smeitink JA, Wevers RA, Wanders RJ: Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene. Am J Hum Genet. 1998 Aug;63(2):329-38. [PubMed Link Image]
  2. Moebius FF, Fitzky BU, Lee JN, Paik YK, Glossmann H: Molecular cloning and expression of the human delta7-sterol reductase. Proc Natl Acad Sci U S A. 1998 Feb 17;95(4):1899-902. [PubMed Link Image]
  3. 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]
  4. Wassif CA, Maslen C, Kachilele-Linjewile S, Lin D, Linck LM, Connor WE, Steiner RD, Porter FD: Mutations in the human sterol delta7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome. Am J Hum Genet. 1998 Jul;63(1):55-62. [PubMed Link Image]
  5. Fitzky BU, Witsch-Baumgartner M, Erdel M, Lee JN, Paik YK, Glossmann H, Utermann G, Moebius FF: Mutations in the Delta7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8181-6. [PubMed Link Image]
  6. Witsch-Baumgartner M, Fitzky BU, Ogorelkova M, Kraft HG, Moebius FF, Glossmann H, Seedorf U, Gillessen-Kaesbach G, Hoffmann GF, Clayton P, Kelley RI, Utermann G: Mutational spectrum in the Delta7-sterol reductase gene and genotype-phenotype correlation in 84 patients with Smith-Lemli-Opitz syndrome. Am J Hum Genet. 2000 Feb;66(2):402-12. [PubMed Link Image]
  7. Krakowiak PA, Nwokoro NA, Wassif CA, Battaile KP, Nowaczyk MJ, Connor WE, Maslen C, Steiner RD, Porter FD: Mutation analysis and description of sixteen RSH/Smith-Lemli-Opitz syndrome patients: polymerase chain reaction-based assays to simplify genotyping. Am J Med Genet. 2000 Sep 18;94(3):214-27. [PubMed Link Image]
  8. Witsch-Baumgartner M, Ciara E, Loffler J, Menzel HJ, Seedorf U, Burn J, Gillessen-Kaesbach G, Hoffmann GF, Fitzky BU, Mundy H, Clayton P, Kelley RI, Krajewska-Walasek M, Utermann G: Frequency gradients of DHCR7 mutations in patients with Smith-Lemli-Opitz syndrome in Europe: evidence for different origins of common mutations. Eur J Hum Genet. 2001 Jan;9(1):45-50. [PubMed Link Image]
  9. Langius FA, Waterham HR, Romeijn GJ, Oostheim W, de Barse MM, Dorland L, Duran M, Beemer FA, Wanders RJ, Poll-The BT: Identification of three patients with a very mild form of Smith-Lemli-Opitz syndrome. Am J Med Genet A. 2003 Sep 15;122(1):24-9. [PubMed Link Image]
Enzyme 4 Metabolite References
  1. Porter FD: Smith-Lemli-Opitz syndrome: pathogenesis, diagnosis and management. Eur J Hum Genet. 2008 May;16(5):535-41. Epub 2008 Feb 20. [PubMed Link Image]
Enzyme 5 [top]
Enzyme 5 ID 5998
Enzyme 5 Name Cytochrome P450 11A1, mitochondrial precursor
Enzyme 5 Synonyms
  1. CYPXIA1
  2. P450(scc
  3. Cholesterol side-chain cleavage enzyme
  4. Cholesterol desmolase
Enzyme 5 Gene Name CYP11A1
Enzyme 5 Protein Sequence >Cytochrome P450 11A1, mitochondrial precursor 
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWL
NLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPER
FLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVS
VLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQM
FHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG
ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAAR
HQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIY
ALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINML
ENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Enzyme 5 Number of Residues 521
Enzyme 5 Molecular Weight 60103
Enzyme 5 Theoretical pI 9.18
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone
Enzyme 5 Pathways
Enzyme 5 Reactions
  • cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 181376 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P05108 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name CP11A_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1566 bp 
ATGCTGGCCAAGGGTCTTCCCCCACGCTCAGTCCTGGTCAAAGGCTACCAGACCTTTCTG
AGTGCCCCCAGGGAGGGGCTGGGGCGTCTCAGGGTGCCCACTGGCGAGGGAGCTGGCATC
TCCACCCGCAGTCCTCGCCCCTTCAATGAGATCCCCTCTCCTGGTGACAATGGCTGGCTA
AACCTGTACCATTTCTGGAGGGAGACGGGCACACACAAAGTCCACCTTCACCATGTCCAG
AATTTCCAGAAGTATGGCCCGATTTACAGGGAGAAGCTCGGCAACGTGGAGTCGGTTTAT
GTCATCGACCCTGAAGATGTGGCCCTTCTCTTTAAGTCCGAGGGCCCCAACCCAGAACGA
TTCCTCATCCCGCCCTGGGTCGCCTATCACCAGTATTACCAGAGACCCATAGGAGTCCTG
TTGAAGAAGTCGGCAGCCTGGAAGAAAGACCGGGTGGCCCTGAACCAGGAGGTGATGGCT
CCAGAGGCCACCAAGAACTTTTTGCCCCTGTTGGATGCAGTGTCTCGGGACTTCGTCAGT
GTCCTGCACAGGCGCATCAAGAAGGCGGGCTCCGGAAATTACTCGGGGGACATCAGTGAT
GACCTGTTCCGCTTTGCCTTTGAGTCCATCACTAACGTCATTTTTGGGGAGCGCCAGGGG
ATGCTGGAGGAAGTAGTGAACCCCGAGGCCCAGCGATTCATTGATGCCATCTACCAGATG
TTCCACACCAGCGTCCCCATGCTCAACCTTCCCCCAGACCTGTTCCGTCTGTTCAGGACC
AAGACCTGGAAGGACCATGTGGCTGCATGGGACGTGATTTTCAGTAAAGCTGACATATAC
ACCCAGAACTTCTACTGGGAATTGAGACAGAAAGGAAGTGTTCACCACGATTACCGTGGC
ATGCTCTACAGACTCCTGGGAGACAGCAAGATGTCCTTCGAGGACATCAAGGCCAACGTC
ACAGAGATGCTGGCAGGAGGGGTGGACACGACGTCCATGACCCTGCAGTGGCACTTGTAT
GAGATGGCACGCAACCTGAAGGTGCAGGATATGCTGCGGGCAGAGGTCTTGGCTGCGCGG
CACCAGGCCCAGGGAGACATGGCCACGATGCTACAGCTGGTCCCCCTCCTCAAAGCCAGC
ATCAAGGAGACACTAAGACTTCACCCCATCTCCGTGACCCTGCAGAGATATCTTGTAAAT
GACTTGGTTCTTCGAGATTACATGATTCCTGCCAAGACACTGGTGCAAGTGGCCATCTAT
GCTCTGGGCCGAGAGCCCACCTTCTTCTTCGACCCGGAAAATTTTGACCCAACCCGATGG
CTGAGCAAAGACAAGAACATCACCTACTTCCGGAACTTGGGCTTTGGCTGGGGTGTGCGG
CAGTGTCTGGGACGGCGGATCGCTGAGCTAGAGATGACCATCTTCCTCATCAATATGCTG
GAGAACTTCAGAGTTGAAATCCAACACCTCAGCGATGTGGGCACCACATTCAACCTCATT
CTGATGCCTGAAAAGCCCATCTCCTTCACCTTCTGGCCCTTTAACCAGGAAGCAACCCAG
CAGTGA
Enzyme 5 GenBank Gene ID M14565 Link Image
Enzyme 5 GeneCard ID CYP11A1 Link Image
Enzyme 5 GenAtlas ID CYP11A1 Link Image
Enzyme 5 HGNC ID HGNC:2590 Link Image
Enzyme 5 Chromosome Location 15
Enzyme 5 Locus 15q23-q24
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Chung BC, Matteson KJ, Voutilainen R, Mohandas TK, Miller WL: Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning, assignment of the gene to chromosome 15, and expression in the placenta. Proc Natl Acad Sci U S A. 1986 Dec;83(23):8962-6. [PubMed Link Image]
  2. Morohashi K, Sogawa K, Omura T, Fujii-Kuriyama Y: Gene structure of human cytochrome P-450(SCC), cholesterol desmolase. J Biochem (Tokyo). 1987 Apr;101(4):879-87. [PubMed Link Image]
  3. Hu MC, Guo IC, Lin JH, Chung BC: Regulated expression of cytochrome P-450scc (cholesterol-side-chain cleavage enzyme) in cultured cell lines detected by antibody against bacterially expressed human protein. Biochem J. 1991 Mar 15;274 ( Pt 3):813-7. [PubMed Link Image]
  4. Matteson KJ, Chung BC, Urdea MS, Miller WL: Study of cholesterol side-chain cleavage (20,22 desmolase) deficiency causing congenital lipoid adrenal hyperplasia using bovine-sequence P450scc oligodeoxyribonucleotide probes. Endocrinology. 1986 Apr;118(4):1296-305. [PubMed Link Image]
  5. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
  6. Tajima T, Fujieda K, Kouda N, Nakae J, Miller WL: Heterozygous mutation in the cholesterol side chain cleavage enzyme (p450scc) gene in a patient with 46,XY sex reversal and adrenal insufficiency. J Clin Endocrinol Metab. 2001 Aug;86(8):3820-5. [PubMed Link Image]
  7. Katsumata N, Ohtake M, Hojo T, Ogawa E, Hara T, Sato N, Tanaka T: Compound heterozygous mutations in the cholesterol side-chain cleavage enzyme gene (CYP11A) cause congenital adrenal insufficiency in humans. J Clin Endocrinol Metab. 2002 Aug;87(8):3808-13. [PubMed Link Image]
Enzyme 5 Metabolite References
  1. Guryev O, Carvalho RA, Usanov S, Gilep A, Estabrook RW: A pathway for the metabolism of vitamin D3: unique hydroxylated metabolites formed during catalysis with cytochrome P450scc (CYP11A1). Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):14754-9. Epub 2003 Dec 1. [PubMed Link Image]
Enzyme 6 [top]
Enzyme 6 ID 7345
Enzyme 6 Name 24-dehydrocholesterol reductase precursor
Enzyme 6 Synonyms
  1. 3-beta- hydroxysterol delta-24-reductase
  2. Seladin-1
  3. Diminuto/dwarf1 homolog
Enzyme 6 Gene Name DHCR24
Enzyme 6 Protein Sequence >24-dehydrocholesterol reductase precursor 
MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKL
SSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMD
ILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKY
GLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKL
RFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYY
KPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVP
PKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQ
PGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREE
FWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH
Enzyme 6 Number of Residues 516
Enzyme 6 Molecular Weight 60102
Enzyme 6 Theoretical pI 8.24
Enzyme 6 GO Classification
Function
—
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Energy production and conversion
Enzyme 6 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 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-22
Enzyme 6 Transmembrane Regions
  • 32-52
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 10442025 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q15392 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DHC24_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID AF261758 Link Image
Enzyme 6 GeneCard ID DHCR24 Link Image
Enzyme 6 GenAtlas ID DHCR24 Link Image
Enzyme 6 HGNC ID HGNC:2859 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p33-p31.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available