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{{PBB|geneid=8630}} |
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'''Hydroxysteroid 17-beta dehydrogenase 6''' is an [[enzyme]] that in humans is encoded by the ''HSD17B6'' [[gene]].<ref name="pmid11165032">{{cite journal | author = Baker ME | title = Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action | journal = Mol Cell Endocrinol | volume = 171 | issue = |
'''Hydroxysteroid 17-beta dehydrogenase 6''' is an [[enzyme]] that in humans is encoded by the ''HSD17B6'' [[gene]].<ref name="pmid11165032">{{cite journal | author = Baker ME | title = Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action | journal = Mol Cell Endocrinol | volume = 171 | issue = 1–2 | pages = 211–5 | year = 2001 | month = Feb | pmid = 11165032 | pmc = | doi =10.1016/S0303-7207(00)00414-7 }}</ref><ref name="pmid19027726">{{cite journal | author = 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 | title = The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative | journal = Chem Biol Interact | volume = 178 | issue = 1–3 | pages = 94–8 | year = 2009 | month = Feb | pmid = 19027726 | pmc = 2896744| doi = 10.1016/j.cbi.2008.10.040 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8630| accessdate = }}</ref> |
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| summary_text = 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.<ref name="entrez" |
| summary_text = 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.<ref name="entrez" /> |
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*{{cite journal | author=Biswas MG, Russell DW |title=Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate |
*{{cite journal | author=Biswas MG, Russell DW |title=Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15959–66 |year= 1997 |pmid= 9188497 |doi=10.1074/jbc.272.25.15959 }} |
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*{{cite journal | author=Huang XF, Luu-The V |title=Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase |
*{{cite journal | author=Huang XF, Luu-The V |title=Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29452–7 |year= 2000 |pmid= 10896656 |doi= 10.1074/jbc.M000562200 }} |
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*{{cite journal | author=Kedishvili NY, Belyaeva OV, Gough WH |title=Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure |
*{{cite journal | author=Kedishvili NY, Belyaeva OV, Gough WH |title=Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure |journal=Chem. Biol. Interact. |volume=130-132 |issue= 1–3 |pages= 457–67 |year= 2001 |pmid= 11306067 |doi=10.1016/S0009-2797(00)00291-X }} |
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*{{cite journal | author=Chetyrkin SV, Hu J, Gough WH, ''et al.'' |title=Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase |
*{{cite journal | author=Chetyrkin SV, Hu J, Gough WH, ''et al.'' |title=Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 1–10 |year= 2001 |pmid= 11360992 |doi= 10.1006/abbi.2000.2203 }} |
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*{{cite journal | author=Huang XF, Luu-The V |title=Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase |
*{{cite journal | author=Huang XF, Luu-The V |title=Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase |journal=Biochim. Biophys. Acta |volume=1520 |issue= 2 |pages= 124–30 |year= 2001 |pmid= 11513953 |doi= }} |
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*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} |
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*{{cite journal | author=Jones MR, Italiano L, Wilson SG, ''et al.'' |title=Polymorphism in HSD17B6 is associated with key features of polycystic ovary syndrome |
*{{cite journal | author=Jones MR, Italiano L, Wilson SG, ''et al.'' |title=Polymorphism in HSD17B6 is associated with key features of polycystic ovary syndrome |journal=Fertil. Steril. |volume=86 |issue= 5 |pages= 1438–46 |year= 2006 |pmid= 17070195 |doi= 10.1016/j.fertnstert.2006.04.027 }} |
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*{{cite journal | author=Belyaeva OV, Chetyrkin SV, Clark AL, ''et al.'' |title=Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and epimerization of 3alpha-hydroxysteroids in human tissues |
*{{cite journal | author=Belyaeva OV, Chetyrkin SV, Clark AL, ''et al.'' |title=Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and epimerization of 3alpha-hydroxysteroids in human tissues |journal=Endocrinology |volume=148 |issue= 5 |pages= 2148–56 |year= 2007 |pmid= 17289849 |doi= 10.1210/en.2006-1491 | pmc=2571913 }} |
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Revision as of 17:57, 12 June 2011
Template:PBB Hydroxysteroid 17-beta dehydrogenase 6 is an enzyme that in humans is encoded by the HSD17B6 gene.[1][2][3]
References
- ^ Baker ME (2001). "Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action". Mol Cell Endocrinol. 171 (1–2): 211–5. doi:10.1016/S0303-7207(00)00414-7. PMID 11165032.
{{cite journal}}
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ignored (help) - ^ 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 (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. PMC 2896744. PMID 19027726.
{{cite journal}}
: Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link) - ^ "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)".