HSD17B6

HSD17B6
Identifiers
Aliases	HSD17B6 , HSE, RODH, SDR9C6, hydroxysteroid (17-beta) dehydrogenase 6, hydroxysteroid 17-beta dehydrogenase 6
External IDs	OMIM: 606623 MGI: 1351670 HomoloGene: 20811 GeneCards: HSD17B6
Gene location (Human)
Chr.	Chromosome 12 (human)
End	56,787,790 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	127,843,480 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; lower lobe of lung; ; seminal vesicula; ; parietal pleura; ; spleen; ; canal of the cervix; ; saphenous vein; ; caudate nucleus; ; nucleus accumbens; ; prostate;
	Top expressed in
	left lobe of liver; ; duodenum; ; olfactory epithelium; ; jejunum; ; epithelium of stomach; ; mucous cell of stomach; ; blastocyst; ; morula; ; intestinal villus; ; pyloric antrum;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	electron transfer activity ; oxidoreductase activity ; estradiol 17-beta-dehydrogenase activity ; catalytic activity ; testosterone dehydrogenase (NAD+) activity ; NAD-retinol dehydrogenase activity ;
Cellular component	organelle membrane ; endosome ; early endosome membrane ; intracellular anatomical structure ; endoplasmic reticulum ; membrane ; intracellular membrane-bounded organelle ;
Biological process	androgen biosynthetic process ; androgen catabolic process ; steroid metabolic process ; lipid metabolism ; electron transport chain ;
	Sources:Amigo / QuickGO
Orthologs
	8630
	27400
	ENSG00000025423
	ENSMUSG00000025396
	O14756
	Q9R092
	NM_003725
	NM_013786 ; NM_001359377
	NP_003716
	NP_038814 ; NP_001346306
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 03, 2024

Hydroxysteroid 17-beta dehydrogenase 6 is an enzyme that in humans is encoded by the HSD17B6 gene.^[5]^[6]^[7]

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.^[7]

Related Research Articles

17β-Hydroxysteroid dehydrogenases, also 17-ketosteroid reductases (17-KSR), are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β-hydroxysteroids in steroidogenesis and steroid metabolism. This includes interconversion of DHEA and androstenediol, androstenedione and testosterone, and estrone and estradiol.

In enzymology, a retinol dehydrogenase (RDH) (EC 1.1.1.105) is an enzyme that catalyzes the chemical reaction

17β-Hydroxysteroid dehydrogenase 1 (17β-HSD1) is an enzyme that in humans is encoded by the HSD17B1 gene. This enzyme oxidizes or reduces the C17 hydroxy/keto group of androgens and estrogens and hence is able to regulate the potency of these sex steroids

HSD3B1 is a human gene that encodes for a 3beta-hydroxysteroid dehydrogenase/delta(5)-delta(4)isomerase type I or hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1. While it can carry out the same function as HSD3B2, it localizes primarily to different tissues, such as the placenta and nonsteroidogenic tissues. Its requirement for the production of progesterone by the placenta, which has a vital role in pregnancy, may be one reason why no disease based on mutations in this gene has been identified to date, besides prostate cancer.

Aldo-keto reductase family 1 member C3 (AKR1C3), also known as 17β-hydroxysteroid dehydrogenase type 5 is a key steroidogenic enzyme that in humans is encoded by the AKR1C3 gene.

Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.

17β-Hydroxysteroid dehydrogenase 2 (17β-HSD2) is an enzyme of the 17β-hydroxysteroid dehydrogenase (17β-HSD) family that in humans is encoded by the HSD17B2 gene.

3α-Hydroxysteroid dehydrogenase is an enzyme that in humans is encoded by the AKR1C4 gene. It is known to be necessary for the synthesis of the endogenous neurosteroids allopregnanolone, THDOC, and 3α-androstanediol. It is also known to catalyze the reversible conversion of 3α-androstanediol (5α-androstane-3α,17β-diol) to dihydrotestosterone and vice versa.

3-keto-steroid reductase is an enzyme that in humans is encoded by the HSD17B7 gene.

Retinol dehydrogenase 11 is an enzyme that in humans is encoded by the RDH11 gene.

Estradiol 17 beta-dehydrogenase 8 is an enzyme that in humans is encoded by the HSD17B8 gene.

Estradiol 17-beta-dehydrogenase 12 is an enzyme that in humans is encoded by the HSD17B12 gene.

Retinol dehydrogenase 14 is an enzyme that in humans is encoded by the RDH14 gene.

Short-chain dehydrogenase/reductase 3 is an enzyme that in humans is encoded by the DHRS3 gene.

Dehydrogenase/reductase SDR family member 9 is an enzyme that in humans is encoded by the DHRS9 gene.

Retinol dehydrogenase 8 is an enzyme that in humans is encoded by the RDH8 gene.

<span class="mw-page-title-main">Epiandrosterone</span> Chemical compound

Epiandrosterone, or isoandrosterone, also known as 3β-androsterone, 3β-hydroxy-5α-androstan-17-one, or 5α-androstan-3β-ol-17-one, is a steroid hormone with weak androgenic activity. It is a metabolite of testosterone and dihydrotestosterone (DHT). It was first isolated in 1931, by Adolf Friedrich Johann Butenandt and Kurt Tscherning. They distilled over 17,000 litres of male urine, from which they got 50 milligrams of crystalline androsterone, which was sufficient to find that the chemical formula was very similar to estrone.

Retinol dehydrogenase 16 (all-trans) is a protein that in humans is encoded by the RDH16 gene. The gene is also known as RODH-4 and SDR9C8.

NADP-retinol dehydrogenase (EC 1.1.1.300, all-trans retinal reductase, all-trans-retinol dehydrogenase, NADP(H)-dependent retinol dehydrogenase/reductase, RDH11, RDH12, RDH13, RDH14, retinol dehydrogenase 12, retinol dehydrogenase 14, retinol dehydrogenase (NADP⁺), RalR1, PSDR1) is an enzyme with systematic name retinol:NADP⁺ oxidoreductase. This enzyme catalyses the following chemical reaction

Retinol dehydrogenase 13 (all-trans/9-cis) is a protein that in humans is encoded by the RDH13 gene. This gene encodes a mitochondrial short-chain dehydrogenase/reductase, which catalyzes the reduction and oxidation of retinoids. The encoded enzyme may function in retinoic acid production and may also protect the mitochondria against oxidative stress. Alternatively spliced transcript variants have been described.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000025423 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025396 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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. doi:10.1016/S0303-7207(00)00414-7. PMID 11165032. S2CID 42947381.
↑ 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. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC 2896744 . PMID 19027726.
1 2 "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)".

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. doi:10.1016/s0167-4781(01)00247-0. 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . 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. PMC 2571913 . PMID 17289849.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000025423 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025396 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11165032-5] 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. doi:10.1016/S0303-7207(00)00414-7. PMID 11165032. S2CID 42947381.

[pmid19027726-6] 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. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC 2896744 . PMID 19027726.

[entrez-7] 1 2 "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)".

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HSD17B6

Related Research Articles

References

Further reading