We are currently updating the database - data may be missing for the next 10 minutes. We apologize for any inconvenience.

Human Metabolome Database Version 2.5

 

Showing metabocard for (24R)-Cholest-5-ene-3-beta,7-alpha,24-triol (HMDB11644)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2009-02-02 11:59:47
Update Date 2009-05-05 21:07:38
Accession Number HMDB11644
Secondary Accession Numbers Not Available
Common Name (24R)-Cholest-5-ene-3-beta,7-alpha,24-triol
Description (24R)-Cholest-5-ene-3-beta,7-alpha,24-triol is a hydroxysterol and a bile acid intermediate. It is produced from the reaction of 24(R)-Hydroxycholesterol with the enzyme CYP39A, which is also known as 24-hydroxycholesterol 7alpha-hydroxylase (EC 1.14.13.99). This enzyme catalyzes the following reaction: (24R)-cholest-5-ene-3beta,24-diol + NADPH + H+ O2 = (24R)-cholest-5-ene-3beta,7alpha,24-triol + NADP+ + H2O. This leads to the 7-alpha hydroxylation of 24(R)-hydroxycholesterol. This enzyme can act on both the 24R and 24S isomers.
Synonyms
  1. 5a-cholesta-7,24-dien-3-b-ol
  2. (24R)-cholest-5-ene 3-b,7-a,24-triol
  3. (24R)-cholest-5-ene-3beta,7alpha,24-triol
  4. 5a-cholesta-7,24-dien-3-beta-ol
Chemical IUPAC Name Not Available
Chemical Formula C27H46O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
Class
Sub Class
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • alkene
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 418.652
Monoisotopic Molecular Weight 418.344696
Isomeric SMILES CC(C)[C@H](O)CC[C@@H](C)C1CC[C@H]2[C@@H]3[C@H](O)C=C4C[C@@H](O)CC[C@]4(C)[C@H]3CC[C@]12C
Canonical SMILES CC(C)C(O)CCC(C)C1CCC2C3C(O)C=C4CC(O)CCC4(C)C3CCC12C
KEGG Compound ID Not Available
BioCyc ID 5-ALPHA-CHOLESTA-724-DIEN-3-BETA-OL Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB11644 Link Image
Metagene Link HMDB11644 Link Image
METLIN ID Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C27H46O3/c1-16(2)23(29)9-6-17(3)20-7-8-21-25-22(11-13-27(20,21)5)26(4)12-10-19(28)14-18(26)15-24(25)30/h15-17,19-25,28-30H,6-14H2,1-5H3/t17-,19+,20?,21+,22+,23-,24-,25+,26+,27-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 8.49e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.28 [Predicted by ALOGPS] 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 Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Bile Acid Biosynthesis SMP00035 Link Image map00120 Link Image
General References Not Available
Metabolic Enzymes
  1. 24-hydroxycholesterol 7-alpha-hydroxylase
Enzyme 1 [top]
Enzyme 1 ID 11444
Enzyme 1 Name 24-hydroxycholesterol 7-alpha-hydroxylase
Enzyme 1 Synonyms
  1. Oxysterol 7-alpha-hydroxylase
  2. Cytochrome P450 39A1
  3. hCYP39A1
Enzyme 1 Gene Name CYP39A1
Enzyme 1 Protein Sequence >24-hydroxycholesterol 7-alpha-hydroxylase
MELISPTVIIILGCLALFLLLQRKNLRRPPCIKGWIPWIGVGFEFGKAPLEFIEKARIKY
GPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRTASIPKNVFLALHEKLY
IMLKGKMGTVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLF
STNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAK
DNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIM
EGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIP
SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFA
LLEVQMCIILILYKYDCSLLDPLPKQSYLHLVGVPQPEGQCRIEYKQRI
Enzyme 1 Number of Residues 469
Enzyme 1 Molecular Weight 54115.3
Enzyme 1 Theoretical pI 8.88
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
Component
Enzyme 1 General Function Involved in monooxygenase activity
Enzyme 1 Specific Function Involved in the bile acid metabolism. Has a preference for 24-hydroxycholesterol, and converts it into a 7-alpha- hydroxylated product
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • (24R)-cholest-5-ene-3beta,24-diol + NADPH + H+ + O2 = (24R)-cholest-5-ene-3beta,7alpha,24-triol + NADP+ + H2O [RN:R07208]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 7533024 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9NYL5 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CP39A_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1410 bp
ATGGAACTAATTTCCCCAACAGTGATTATAATCCTGGGTTGCCTTGCTCTGTTCTTACTC
CTTCAGCGGAAGAATTTGCGTAGACCCCCGTGCATCAAGGGCTGGATTCCTTGGATTGGA
GTTGGATTTGAGTTTGGGAAAGCCCCTCTAGAATTTATAGAGAAAGCAAGAATCAAGTAT
GGACCAATATTTACAGTCTTTGCTATGGGAAACCGAATGACCTTTGTTACTGAAGAAGAA
GGAATTAATGTGTTTCTAAAATCCAAAAAAGTAGATTTTGAACTAGCAGTGCAAAATATC
GTTTATCGTACAGCATCAATTCCAAAGAATGTCTTTTTAGCACTGCATGAAAAACTCTAT
ATTATGTTGAAAGGGAAAATGGGGACTGTCAATCTCCATCAGTTTACTGGGCAACTGACT
GAAGAATTACATGAACAACTGGAGAATTTAGGCACTCATGGGACAATGGACCTGAACAAC
TTAGTAAGACATCTCCTTTATCCAGTCACAGTGAATATGCTCTTTAATAAAAGTTTGTTT
TCCACAAACAAGAAAAAAATCAAGGAGTTCCATCAGTATTTTCAAGTTTATGATGAAGAT
TTTGAGTATGGGTCCCAGTTGCCAGAGTGTCTTCTAAGAAACTGGTCAAAATCCAAAAAG
TGGTTCCTGGAACTGTTTGAGAAAAACATTCCAGATATAAAAGCATGTAAATCTGCAAAA
GATAATTCCATGACATTATTGCAAGCTACGCTGGATATTGTAGAGACGGAAACAAGTAAG
GAAAACTCACCCAATTATGGGCTCTTACTGCTTTGGGCTTCTCTGTCTAATGCTGTTCCT
GTTGCATTTTGGACACTTGCATACGTCCTTTCTCATCCTGATATCCACAAGGCCATTATG
GAAGGCATATCTTCTGTGTTTGGCAAAGCAGGCAAAGATAAGATTAAAGTGTCTGAGGAT
GACCTGGAGAAACTCCTTCTAATTAAATGGTGTGTTTTGGAAACCATTCGTTTAAAAGCT
CCTGGTGTCATTACTAGAAAAGTGGTGAAGCCTGTGGAAATTTTGAATTACATCATTCCT
TCTGGTGACTTGTTGATGTTGTCTCCATTTTGGCTGCATAGAAATCCAAAGTATTTTCCT
GAGCCTGAATTGTTCAAACCTGAACGTTGGAAAAAGGCAAATTTAGAGAAGCACTCTTTC
TTGGACTGCTTCATGGCATTTGGAAGCGGGAAGTTCCAGTGTCCTGCAAGGTGGTTTGCT
CTGTTAGAGGTTCAGATGTGTATTATTTTAATACTTTATAAATATGACTGTAGTCTTCTG
GACCCATTACCCAAACAGAGTTATCTCCATTTGGTGGGTGTCCCCCAGCCGGAAGGGCAA
TGCCGAATTGAATATAAACAAAGAATATGA
Enzyme 1 GenBank Gene ID AF237982 Link Image
Enzyme 1 GeneCard ID CYP39A1 Link Image
Enzyme 1 GenAtlas ID CYP39A1 Link Image
Enzyme 1 HGNC ID HGNC:17449 Link Image
Enzyme 1 Chromosome Location 6
Enzyme 1 Locus 6p21.1-p11.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Li-Hawkins J, Lund EG, Bronson AD, Russell DW: Expression cloning of an oxysterol 7alpha-hydroxylase selective for 24-hydroxycholesterol. J Biol Chem. 2000 Jun 2;275(22):16543-9. [PubMed Link Image]
  2. 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]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [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]
Enzyme 1 Metabolite References Not Available