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Hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)
Identifiers
Symbols HSD17B6; HSE; RODH
External IDs OMIM606623 MGI1351670 HomoloGene20811 GeneCards: HSD17B6 Gene
RNA expression pattern
PBB GE HSD17B6 37512 at tn.png
PBB GE HSD17B6 205700 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 8630 27400
Ensembl ENSG00000025423 ENSMUSG00000025396
UniProt n/a n/a
RefSeq (mRNA) NM_003725 XM_988102
RefSeq (protein) NP_003716 XP_993196
Location (UCSC) Chr 12:
55.44 - 55.47 Mb
Chr 10:
127.39 - 127.4 Mb
PubMed search [1] [2]

Hydroxysteroid 17-beta dehydrogenase 6 is an enzyme that in humans is encoded by the HSD17B6 gene.[1][2][3]

The protein encoded by this gene has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activity can convert androsterone to epi-androsterone. Both reactions use NAD+ as the preferred cofactor. This gene is a member of the retinol dehydrogenase family. Transcript variants utilizing alternative polyadenylation signals exist.[3]

References

  1. ^ Baker ME (Feb 2001). "Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action". Mol Cell Endocrinol 171 (1-2): 211-5. PMID 11165032.  
  2. ^ Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Feb 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact 178 (1-3): 94-8. doi:10.1016/j.cbi.2008.10.040. PMID 19027726.  
  3. ^ a b "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8630.  

Further reading

  • Biswas MG, Russell DW (1997). "Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate.". J. Biol. Chem. 272 (25): 15959–66. doi:10.1074/jbc.272.25.15959. PMID 9188497.  
  • Huang XF, Luu-The V (2000). "Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase.". J. Biol. Chem. 275 (38): 29452–7. doi:10.1074/jbc.M000562200. PMID 10896656.  
  • Kedishvili NY, Belyaeva OV, Gough WH (2001). "Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure.". Chem. Biol. Interact. 130-132 (1-3): 457–67. doi:10.1016/S0009-2797(00)00291-X. PMID 11306067.  
  • Chetyrkin SV, Hu J, Gough WH, et al. (2001). "Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase.". Arch. Biochem. Biophys. 386 (1): 1–10. doi:10.1006/abbi.2000.2203. PMID 11360992.  
  • Huang XF, Luu-The V (2001). "Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase.". Biochim. Biophys. Acta 1520 (2): 124–30. PMID 11513953.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  
  • Jones MR, Italiano L, Wilson SG, et al. (2006). "Polymorphism in HSD17B6 is associated with key features of polycystic ovary syndrome.". Fertil. Steril. 86 (5): 1438–46. doi:10.1016/j.fertnstert.2006.04.027. PMID 17070195.  
  • Belyaeva OV, Chetyrkin SV, Clark AL, et al. (2007). "Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and epimerization of 3alpha-hydroxysteroids in human tissues.". Endocrinology 148 (5): 2148–56. doi:10.1210/en.2006-1491. PMID 17289849.  
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