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Human Metabolome Database Version 2.5

 

Showing metabocard for 5b-Dihydrotestosterone (HMDB06770)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2008-08-06 17:25:44
Update Date 2009-05-05 21:01:10
Accession Number HMDB06770
Secondary Accession Numbers Not Available
Common Name 5b-Dihydrotestosterone
Description 5beta-Dihydrotestosterone is an intermediate in Androgen and estrogen metabolism. 5beta-Dihydrotestosterone is generated from Testosterone via the enzyme 3-oxo-5beta-steroid 4-dehydrogenase (EC 1.3.99.6).
Synonyms
  1. 17beta-hydroxy-5beta-androstan-3-one
  2. 5beta-Dihydrotestosterone
Chemical IUPAC Name (5R,8R,9S,10S,13S,14S,17S)-17-hydroxy-10,13-dimethyl-1,2,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydrocyclopenta[a]phenanthren-3-one
Chemical Formula C19H30O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • ketone
  • secondary alcohol
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 290.440
Monoisotopic Molecular Weight 290.224579
Isomeric SMILES C[C@]12CC[C@H]3[C@@H](CC[C@@H]4CC(=O)CC[C@]34C)[C@@H]1CC[C@@H]2O
Canonical SMILES CC12CCC3C(CCC4CC(=O)CCC34C)C1CCC2O
KEGG Compound ID C05293 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB06770 Link Image
Metagene Link HMDB06770 Link Image
METLIN ID Not Available
PubChem Compound 11302 Link Image
PubChem Substance Not Available
ChEBI ID Not Available
CAS Registry Number 571-22-2
InChI Identifier InChI=1/C19H30O2/c1-18-9-7-13(20)11-12(18)3-4-14-15-5-6-17(21)19(15,2)10-8-16(14)18/h12,14-17,21H,3-11H2,1-2H3/t12-,14+,15+,16+,17+,18+,19+/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 9.98e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 3.37 [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 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 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
Androgen and Estrogen Metabolism SMP00068 Link Image map00150 Link Image
General References Not Available
Metabolic Enzymes
  1. 3-oxo-5-beta-steroid 4-dehydrogenase
Enzyme 1 [top]
Enzyme 1 ID 5822
Enzyme 1 Name 3-oxo-5-beta-steroid 4-dehydrogenase
Enzyme 1 Synonyms
  1. Aldo-keto reductase family 1 member D1
  2. Delta(4)-3-ketosteroid 5-beta-reductase
  3. Delta(4)-3-oxosteroid 5-beta-reductase
Enzyme 1 Gene Name AKR1D1
Enzyme 1 Protein Sequence >3-oxo-5-beta-steroid 4-dehydrogenase
MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQN
EHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIE
VPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELIL
NKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLK
DALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIE
ALNKNVRFVELLMWRDHPEYPFHDEY
Enzyme 1 Number of Residues 326
Enzyme 1 Molecular Weight 37376.6
Enzyme 1 Theoretical pI 7.58
Enzyme 1 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7- alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4- cholesten-3-one can also act as substrates
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) 5beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH + H+ [RN:R02609]
  • (2) 17,21-dihydroxy-5beta-pregnane-3,11,20-trione + NADP+ = cortisone + NADPH + H+ [RN:R02893]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 431857 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P51857 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AK1D1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >981 bp
ATGGATCTCAGTGCTGCAAGTCACCGCATACCTCTAAGTGATGGAAACAGCATTCCCATC
ATCGGACTTGGTACCTACTCAGAACCTAAATCGACCCCTAAGGGAGCCTGTGCAACATCG
GTGAAGGTTGCTATTGACACAGGGTACCGACATATTGATGGGGCCTACATCTACCAAAAT
GAACACGAAGTTGGGGAGGCCATCAGGGAGAAGATAGCAGAAGGAAAGGTGCGGAGGGAA
GATATCTTCTACTGTGGAAAGCTATGGGCTACAAATCATGTCCCAGAGATGGTCCGCCCA
ACCCTGGAGAGGACACTCAGGGTCCTCCAGCTAGATTATGTGGATCTTTACATCATTGAA
GTACCCATGGCCTTTAAGCCAGGAGATGAAATATACCCTAGAGATGAGAATGGCAAATGG
TTATATCACAAGTCAAATCTGTGTGCCACTTGGGAGGCGATGGAAGCTTGCAAAGACGCT
GGCTTGGTGAAATCCCTGGGAGTGTCCAATTTTAACCGCAGGCAGCTGGAGCTCATCCTG
AACAAGCCAGGACTCAAACACAAGCCAGTCAGCAACCAGGTTGAGTGCCATCCGTATTTC
ACCCAGCCAAAACTCTTGAAATTTTGCCAACAACATGACATTGTCATTACTGCATATAGC
CCTTTGGGGACCAGTAGGAATCCAATCTGGGTGAATGTTTCTTCTCCACCTTTGTTAAAG
GATGCACTTCTAAACTCATTGGGGAAAAGGTACAATAAGACAGCAGCTCAAATTGTTTTG
CGTTTCAACATCCAGCGAGGGGTGGTTGTCATTCCTAAAAGCTTTAATCTTGAAAGGATC
AAAGAAAATTTTCAGATCTTTGACTTTTCTCTCACTGAAGAAGAAATGAAGGACATTGAA
GCCTTGAATAAAAATGTCCGCTTTGTAGAATTGCTCATGTGGCGCGATCATCCTGAATAC
CCATTTCATGATGAATACTGA
Enzyme 1 GenBank Gene ID Z28339 Link Image
Enzyme 1 GeneCard ID AKR1D1 Link Image
Enzyme 1 GenAtlas ID AKR1D1 Link Image
Enzyme 1 HGNC ID HGNC:388 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7q32-q33
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjoblom P, Setoguchi T, Okuda KI, Bjorkhem I: Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme. Eur J Biochem. 1994 Jan 15;219(1-2):357-63. [PubMed Link Image]
  2. Charbonneau A, The VL: Genomic organization of a human 5beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim Biophys Acta. 2001 Jan 26;1517(2):228-35. [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. 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]
  5. 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]
  6. Di Costanzo L, Drury JE, Penning TM, Christianson DW: Crystal structure of human liver Delta4-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis. J Biol Chem. 2008 Jun 13;283(24):16830-9. Epub 2008 Apr 11. [PubMed Link Image]
  7. Lemonde HA, Custard EJ, Bouquet J, Duran M, Overmars H, Scambler PJ, Clayton PT: Mutations in SRD5B1 (AKR1D1), the gene encoding delta(4)-3-oxosteroid 5beta-reductase, in hepatitis and liver failure in infancy. Gut. 2003 Oct;52(10):1494-9. [PubMed Link Image]
  8. Gonzales E, Cresteil D, Baussan C, Dabadie A, Gerhardt MF, Jacquemin E: SRD5B1 (AKR1D1) gene analysis in delta(4)-3-oxosteroid 5beta-reductase deficiency: evidence for primary genetic defect. J Hepatol. 2004 Apr;40(4):716-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available