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Human Metabolome Database Version 2.5

 

Showing metabocard for 5-b-Cholestane-3a ,7a ,12a-triol (HMDB01457)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:47
Accession Number HMDB01457
Secondary Accession Numbers Not Available
Common Name 5-b-Cholestane-3a ,7a ,12a-triol
Description 5-b-Cholestane-3a ,7a ,12a-triol is an intermediate in Bile acid biosynthesis. 5-b-Cholestane-3a ,7a ,12a-triol is the second to last step of synthesis of 5beta-Cyprinolsulfate. It is converted from 7alpha,12alpha-Dihydroxy-5beta-cholestan-3-one via enzymatic reaction then it is coneverted to 3alpha,7alpha,12alpha,26-Tetrahydroxy-5beta-cholestane via the enzyme cytochrome P450(EC.1.14.13.15). This compound inhibits la-Hydroxylation, (PMID: 7937829). It is the byproduct of Cholestanetetraol 26-dehydrogenase (EC 1.1.1.161), and the reaction that cataylzes it is classified as a small molecule reaction. (BioCyc)
Synonyms
  1. 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol
  2. 3alpha,7alpha,12alpha-Trihydroxycoprostane
  3. 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholestane
Chemical IUPAC Name 10,13-dimethyl-17-(6-methylheptan-2-yl)-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthrene-3,7,12-triol
Chemical Formula C27H48O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Trihydroxy steroids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
Biofunction
  • Hormones, Membrane component
Application
—
Source
  • Endogenous
Average Molecular Weight 420.668
Monoisotopic Molecular Weight 420.360352
Isomeric SMILES CC(C)CCC[C@@H](C)[C@H]1CC[C@H]2[C@@H]3[C@H](O)C[C@@H]4C[C@H](O)CC[C@]4(C)[C@H]3C[C@H](O)[C@]12C
Canonical SMILES CC(C)CCCC(C)C1CCC2C3C(O)CC4CC(O)CCC4(C)C3CC(O)C12C
KEGG Compound ID C05454 Link Image
BioCyc ID 5-BETA-CHOLESTANE-3-ALPHA7-TETRAOL Link Image
BiGG ID 45846 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01457 Link Image
Metagene Link HMDB01457 Link Image
METLIN ID 6254 Link Image
PubChem Compound 160520 Link Image
PubChem Substance 7851352 Link Image
ChEBI ID Not Available
CAS Registry Number Not Available
InChI Identifier InChI=1/C27H48O3/c1-16(2)7-6-8-17(3)20-9-10-21-25-22(15-24(30)27(20,21)5)26(4)12-11-19(28)13-18(26)14-23(25)29/h16-25,28-30H,6-15H2,1-5H3/t17-,18+,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 5.34e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 4.78 [Predicted by ALOGPS]; 6.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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 (Predicted from LogP)
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
  1. Shimazu K, Kuwabara M, Yoshii M, Kihira K, Takeuchi H, Nakano I, Ozawa S, Onuki M, Hatta Y, Hoshita T: Bile alcohol profiles in bile, urine, and feces of a patient with cerebrotendinous xanthomatosis. J Biochem (Tokyo). 1986 Feb;99(2):477-83. [PubMed Link Image]
  2. Oftebro H, Bjorkhem I, Skrede S, Schreiner A, Pederson JI: Cerebrotendinous xanthomatosis: a defect in mitochondrial 26-hydroxylation required for normal biosynthesis of cholic acid. J Clin Invest. 1980 Jun;65(6):1418-30. [PubMed Link Image]
Metabolic Enzymes
  1. Aldo-keto reductase family 1 member C4
  2. cDNA FLJ76781, highly similar to Homo sapiens cytochrome P450, family 27, subfamily A, polypeptide 1
Enzyme 1 [top]
Enzyme 1 ID 5303
Enzyme 1 Name Aldo-keto reductase family 1 member C4
Enzyme 1 Synonyms
  1. Chlordecone reductase
  2. CDR
  3. 3-alpha-hydroxysteroid dehydrogenase type I
  4. 3-alpha-HSD1
  5. Dihydrodiol dehydrogenase 4
  6. DD4
  7. HAKRA
Enzyme 1 Gene Name AKR1C4
Enzyme 1 Protein Sequence >Aldo-keto reductase family 1 member C4 
MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPM
ALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKP
GLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN
RNYRYVVMDFLMDHPDYPFSDEY
Enzyme 1 Number of Residues 323
Enzyme 1 Molecular Weight 37095
Enzyme 1 Theoretical pI 7.19
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
—
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha- androstan-3alpha,17beta-diol (3-alpha-diol). Also has some 20- alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route
Enzyme 1 Pathways
Enzyme 1 Reactions
  • chlordecone alcohol + NADP+ = chlordecone + NADPH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4261710 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P17516 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AK1C4_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >972 bp 
ATGGATCCCAAATATCAGCGTGTAGAGCTAAATGATGGTCATTTCATGCCCGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGGAACAGAGCTGTAGAGGTCACCAAATTA
GCAATAGAAGCTGGCTTCCGCCATATTGATTCTGCTTATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCACTTTCTTTCAACCACAGATGGTCCAACCAGCCTTGGAA
AGCTCACTGAAAAAACTTCAACTGGACTATGTTGACCTCTATCTTCTTCATTTCCCAATG
GCTCTCAAGCCAGGTGAGACGCCACTACCAAAAGATGAAAATGGAAAAGTAATATTCGAC
ACAGTGGATCTCTCTGCCACATGGGAGGTCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCAAACTTCAACTGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCTTACCTCAACCAGAGC
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCCACAGTGCTCTGGGA
ACCCAACGACATAAACTATGGGTGGACCCAAACTCCCCAGTTCTTTTGGAGGACCCAGTT
CTTTGTGCCTTAGCAAAGAAACACAAACGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGGATCAGAGAGAAC
ATCCAGGTTTTTGAATTCCAGTTGACATCAGAGGATATGAAAGTTCTAGATGGTCTAAAC
AGAAATTATCGATATGTTGTCATGGATTTTCTTATGGACCATCCTGATTATCCATTTTCA
GATGAATATTAG
Enzyme 1 GenBank Gene ID S68287 Link Image
Enzyme 1 GeneCard ID AKR1C4 Link Image
Enzyme 1 GenAtlas ID AKR1C4 Link Image
Enzyme 1 HGNC ID HGNC:387 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10p15-p14
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed Link Image]
  2. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed Link Image]
  3. Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed Link Image]
  4. Kume T, Iwasa H, Shiraishi H, Yokoi T, Nagashima K, Otsuka M, Terada T, Takagi T, Hara A, Kamataki T: Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver. Pharmacogenetics. 1999 Dec;9(6):763-71. [PubMed Link Image]
  5. Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed Link Image]
  6. Dufort I, Labrie F, Luu-The V: Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J Clin Endocrinol Metab. 2001 Feb;86(2):841-6. [PubMed Link Image]
  7. Winters CJ, Molowa DT, Guzelian PS: Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry. 1990 Jan 30;29(4):1080-7. [PubMed Link Image]
  8. Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed Link Image]
  9. Binstock JM, Iyer RB, Hamby CV, Fried VA, Schwartz IS, Weinstein BI, Southren AL: Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase. Biochem Biophys Res Commun. 1992 Sep 16;187(2):760-6. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13003
Enzyme 2 Name cDNA FLJ76781, highly similar to Homo sapiens cytochrome P450, family 27, subfamily A, polypeptide 1
Enzyme 2 Synonyms
  1. CYP27A1, mRNA
  2. Cytochrome P450, family 27, subfamily A, polypeptide 1, isoform CRA_b
Enzyme 2 Gene Name CYP27A1
Enzyme 2 Protein Sequence >cDNA FLJ76781, highly similar to Homo sapiens cytochrome P450, family 27, subfamily A, polypeptide 1 
MAALGCARLRWALRGAGRGLCPHGARAKAAIPAALPSDKATGAPGAGPGVRRRQRSLEEI
PRLGQLRFFFQLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQ
EGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAALYTDAFNE
VIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTF
VRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAA
GPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEA
LHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPK
NTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSVPFGYGVRACLGRR
IAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQFLQRQC
Enzyme 2 Number of Residues 531
Enzyme 2 Molecular Weight 60236
Enzyme 2 Theoretical pI 9.16
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 158261859 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A8K303 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A8K303_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 AK290418 Link Image
Enzyme 2 GeneCard ID A8K303 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