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Human Metabolome Database Version 2.5

 

Showing metabocard for 22b-Hydroxycholesterol (HMDB04035)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 10:27:14
Update Date 2011-09-06 15:38:19
Accession Number HMDB04035
Secondary Accession Numbers Not Available
Common Name 22b-Hydroxycholesterol
Description 22beta-Hydroxycholesterol is a substrate for DCC-interacting protein 13 beta.
Synonyms
  1. (3beta,22R)-Cholest-5-ene-3,22-diol
  2. 22R-hydroxycholesterol
  3. cholest-5-en-3beta,22R-diol
  4. 22beta-Hydroxycholesterol
Chemical IUPAC Name (3S,8S,9S,10R,13R,14S,17R)-17-[(2S,3R)-3-hydroxy-6-methyl-heptan-2-yl]-10,13-dimethyl-2,3,4,7,8,9,11,12,14,15,16,17-dodecahydro-1H-cyclopenta[a]phenanthren-3-ol
Chemical Formula C27H46O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Dihydroxy steroids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • alkene
Biofunction
  • Hormones, Membrane component
Application
Source
  • Endogenous
Average Molecular Weight 402.653
Monoisotopic Molecular Weight 402.349792
Isomeric SMILES CC(C)CC[C@@H](O)[C@@H](C)[C@H]1CC[C@H]2[C@@H]3CC=C4C[C@@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(C)CCC(O)C(C)C1CCC2C3CC=C4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID C05502 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB04035 Link Image
Metagene Link HMDB04035 Link Image
METLIN ID 7006 Link Image
PubChem Compound 167685 Link Image
PubChem Substance 7855 Link Image
ChEBI ID Not Available
CAS Registry Number 22348-64-7
InChI Identifier InChI=1/C27H46O2/c1-17(2)6-11-25(29)18(3)22-9-10-23-21-8-7-19-16-20(28)12-14-26(19,4)24(21)13-15-27(22,23)5/h7,17-18,20-25,28-29H,6,8-16H2,1-5H3/t18-,20-,21-,22+,23-,24-,25+,26-,27+/m0/s1
Synthesis Reference Koreeda, Masato; Ricca, Daniel J. Chirality transfer in stereoselective synthesis. A highly stereocontrolled synthesis of 22-hydroxylated steroid side chains via the [2,3]-Wittig rearrangement. Journal of Organic Chemistry (1986), 51(21), 4090-2.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 6.53e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 5.69 [Predicted by ALOGPS]; 6.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
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)
Biofluid Location Not Available
Tissue Location
Tissue References
Adrenal Cortex
Epidermis
Fibroblasts
Neuron
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroidogenesis SMP00130 Link Image map00140 Link Image
General References
  1. Haidar B, Denis M, Marcil M, Krimbou L, Genest J Jr: Apolipoprotein A-I activates cellular cAMP signaling through the ABCA1 transporter. J Biol Chem. 2004 Mar 12;279(11):9963-9. Epub 2003 Dec 29. [PubMed Link Image]
  2. Yao ZX, Brown RC, Teper G, Greeson J, Papadopoulos V: 22R-Hydroxycholesterol protects neuronal cells from beta-amyloid-induced cytotoxicity by binding to beta-amyloid peptide. J Neurochem. 2002 Dec;83(5):1110-9. [PubMed Link Image]
  3. Matsuzaki J, Tsuji T, Imazeki I, Ikeda H, Nishimura T: Immunosteroid as a regulator for Th1/Th2 balance: its possible role in autoimmune diseases. Autoimmunity. 2005 Aug;38(5):369-75. [PubMed Link Image]
  4. Tuckey RC: Cholesterol side-chain cleavage by mitochondria from the human placenta. Studies using hydroxycholesterols as substrates. J Steroid Biochem Mol Biol. 1992 Sep;42(8):883-90. [PubMed Link Image]
  5. Hanley K, Ng DC, He SS, Lau P, Min K, Elias PM, Bikle DD, Mangelsdorf DJ, Williams ML, Feingold KR: Oxysterols induce differentiation in human keratinocytes and increase Ap-1-dependent involucrin transcription. J Invest Dermatol. 2000 Mar;114(3):545-53. [PubMed Link Image]
Metabolic Enzymes
  1. Cholesterol side-chain cleavage enzyme, mitochondrial
  2. cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
Enzyme 1 [top]
Enzyme 1 ID 5998
Enzyme 1 Name Cholesterol side-chain cleavage enzyme, mitochondrial
Enzyme 1 Synonyms
  1. CYPXIA1
  2. Cholesterol desmolase
  3. Cytochrome P450 11A1
  4. Cytochrome P450(scc)
Enzyme 1 Gene Name CYP11A1
Enzyme 1 Protein Sequence >Cholesterol side-chain cleavage enzyme, mitochondrial
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWL
NLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPER
FLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVS
VLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQM
FHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG
ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAAR
HQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIY
ALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINML
ENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Enzyme 1 Number of Residues 521
Enzyme 1 Molecular Weight 60101.9
Enzyme 1 Theoretical pI 9.18
Enzyme 1 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
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in monooxygenase activity
Enzyme 1 Specific Function Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone
Enzyme 1 Pathways
Enzyme 1 Reactions
  • cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone + 4-methylpentanal + oxidized adrenal ferredoxin + H2O [RN:R02724]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 158258032 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P05108 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CP11A_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1566 bp
ATGCTGGCCAAGGGTCTTCCCCCACGCTCAGTCCTGGTCAAAGGCTGCCAGACCTTTCTG
AGTGCCCCCAGGGAGGGGCTGGGGCGTCTCAGGGTGCCCACTGGCGAGGGAGCTGGCATC
TCCACCCGCAGTCCTCGCCCCTTCAATGAGATCCCCTCTCCTGGTGACAATGGCTGGCTA
AACCTGTACCATTTCTGGAGGGAGACGGGCACACACAAAGTCCACCTTCACCATGTCCAG
AATTTCCAGAAGTATGGCCCGATTTACAGGGAGAAGCTCGGCAACGTGGAGTCGGTTTAT
GTCATCGACCCTGAAGATGTGGCCCTTCTCTTTAAGTCCGAGGGCCCCAACCCAGAACGA
TTCCTCATCCCGCCCTGGGTCGCCTATCACCAGTATTACCAGAGACCCATAGGAGTCCTG
TTGAAGAAGTCGGCAGCCTGGAAGAAAGACCGGGTGGCCCTGAACCAGGAGGTGATGGCT
CCAGAGGCCACCAAGAACTTTTTGCCCCTGTTGGATGCAGTGTCTCGGGACTTCGTCAGT
GTCCTGCACAGGCGCATCAAGAAGGCGGGCTCCGGAAATTACTCGGGGGACATCAGTGAT
GACCTGTTCCGCTTTGCCTTTGAGTCCATCACTAACGTCATTTTTGGGGAGCGCCAGGGG
ATGCTGGAGGAAGTAGTGAACCCCGAGGCCCAGCGATTCATTGATGCCATCTACCAGATG
TTCCACACCAGCGTCCCCATGCTCAACCTTCCCCCAGACCTGTTCCGTCTGTTCAGGACC
AAGACCTGGAAGGACCATGTGGCTGCATGGGACGTGATTTTCAGTAAAGCTGACATATAC
ACCCAGAACTTCTACTGGGAATTGAGACAGAAAGGAAGTGTTCACCACGATTACCGTGGC
ATCCTCTACAGACTCCTGGGAGACAGCAAGATGTCCTTCGAGGACATCAAGGCCAACGTC
ACAGAGATGCTGGCAGGAGGGGTGGACACGACGTCCATGACCCTGCAGTGGCACTTGTAT
GAGATGGCACGCAACCTGAAGGTGCAGGATATGCTGCGGGCAGAGGTCTTGGCTGCGCGG
CACCAGGCCCAGGGAGACATGGCCACGATGCTACAGCTGGTCCCCCTCCTCAAAGCCAGC
ATCAAGGAGACACTAAGACTTCACCCCATCTCCGTGACCCTGCAGAGATATCTTGTAAAT
GACTTGGTTCTTCGAGATTACATGATTCCTGCCAAGACACTGGTGCAAGTGGCCATCTAT
GCTCTGGGCCGAGAGCCCACCTTCTTCTTCGACCCGGAAAATTTTGACCCAACCCGATGG
CTGAGCAAAGACAAGAACATCACCTACTTCCGGAACTTGGGCTTTGGCTGGGGTGTGCGG
CAGTGTCTGGGACGGCGGATCGCTGAGCTAGAGATGACCATCTTCCTCATCAATATGCTG
GAGAACTTCAGAGTTGAAATCCAACACCTCAGCGATGTGGGCACCACATTCAACCTCATT
CTGATGCCTGAAAAGCCCATCTCCTTCACCTTCTGGCCCTTTAACCAGGAAGCAACCCAG
CAGTGA
Enzyme 1 GenBank Gene ID AK292300 Link Image
Enzyme 1 GeneCard ID CYP11A1 Link Image
Enzyme 1 GenAtlas ID CYP11A1 Link Image
Enzyme 1 HGNC ID HGNC:2590 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 15q23-q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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. 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. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13012
Enzyme 2 Name cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
Enzyme 2 Synonyms
  1. CYP11A1, mRNA
  2. Cytochrome P450, family 11, subfamily A, polypeptide 1, isoform CRA_b
Enzyme 2 Gene Name CYP11A1
Enzyme 2 Protein Sequence >cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWL
NLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPER
FLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVS
VLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQM
FHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG
ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAAR
HQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIY
ALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINML
ENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Enzyme 2 Number of Residues 521
Enzyme 2 Molecular Weight 60103
Enzyme 2 Theoretical pI 9.18
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 158258032 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A8K8D5 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A8K8D5_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AK292300 Link Image
Enzyme 2 GeneCard ID A8K8D5 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available