HSD17B4

From Wikipedia, the free encyclopedia

Hydroxysteroid (17-beta) dehydrogenase 4

PDB rendering based on 1ikt.

Available structures: 1ikt, 1s9c, 1zbq

Identifiers

Symbol(s)

HSD17B4; MFE-2

External IDs

OMIM: 601860 MGI: 105089 HomoloGene: 358

Gene ontology
Molecular Function:	• 3-hydroxyacyl-CoA dehydrogenase activity • estradiol 17-beta-dehydrogenase activity • sterol carrier activity • sterol transporter activity • oxidoreductase activity • lyase activity • isomerase activity
Cellular Component:	• mitochondrion • peroxisome
Biological Process:	• lipid metabolic process • fatty acid metabolic process • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000414 (mRNA)
NP_000405 (protein)

NM_008292 (mRNA)
NP_032318 (protein)

Location

Chr 5: 118.82 - 118.91 Mb

Chr 18: 50.25 - 50.32 Mb

Pubmed search

[1]

[2]

Hydroxysteroid (17-beta) dehydrogenase 4, also known as HSD17B4, is a human gene.^[1]

The HSD17B4 gene encodes an enzyme involved in peroxisomal fatty acid beta-oxidation. It was first identified as a 17-beta-estradiol dehydrogenase (Leenders et al., 1996; van Grunsven et al., 1998). Peroxisomal beta-oxidation of fatty acids, originally described by Lazarow and de Duve (1976), is catalyzed by 3 enzymes: acyl-CoA oxidase (see, e.g., ACOX1, MIM 609751); the 'D-bifunctional enzyme,' with enoyl-CoA-hydratase and D-3-hydroxyacyl-CoA dehydrogenase activity, and 3-ketoacyl-CoA thiolase (MIM 604054). See also the L-bifunctional peroxisomal protein (EHHADH; MIM 607037). The D- and L-bifunctional proteins have different substrate specificities. The D-bifunctional protein catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids and also acts in shortening cholesterol for bile acid formation. In contrast, the L-specific bifunctional protein does not have the latter 2 activities (Jiang et al., 1997).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4.

[edit] Further reading

de Launoit Y, Adamski J (1999). "Unique multifunctional HSD17B4 gene product: 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome.". J. Mol. Endocrinol. 22 (3): 227–40. PMID 10343282.
Huyghe S, Mannaerts GP, Baes M, Van Veldhoven PP (2006). "Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model.". Biochim. Biophys. Acta 1761 (9): 973–94. doi:10.1016/j.bbalip.2006.04.006. PMID 16766224.
Palosaari PM, Hiltunen JK (1990). "Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities.". J. Biol. Chem. 265 (5): 2446–9. PMID 2303409.
Adamski J, Normand T, Leenders F, et al. (1995). "Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV.". Biochem. J. 311 ( Pt 2): 437–43. PMID 7487879.
Markus M, Husen B, Adamski J (1996). "The subcellular localization of 17 beta-hydroxysteroid dehydrogenase type 4 and its interaction with actin.". J. Steroid Biochem. Mol. Biol. 55 (5-6): 617–21. PMID 8547189.
Jiang LL, Kobayashi A, Matsuura H, et al. (1997). "Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.". J. Biochem. 120 (3): 624–32. PMID 8902629.
Leenders F, Prescher G, Dolez V, et al. (1997). "Assignment of human 17 beta-hydroxysteroid dehydrogenase IV to chromosome 5q2 by fluorescence in situ hybridization.". Genomics 37 (3): 403–4. PMID 8938456.
Jiang LL, Miyazawa S, Souri M, Hashimoto T (1997). "Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein.". J. Biochem. 121 (2): 364–9. PMID 9089413.
Jiang LL, Kurosawa T, Sato M, et al. (1997). "Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein.". J. Biochem. 121 (3): 506–13. PMID 9133619.
Novikov D, Dieuaide-Noubhani M, Vermeesch JR, et al. (1997). "The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping.". Biochim. Biophys. Acta 1360 (3): 229–40. PMID 9197465.
Suzuki Y, Jiang LL, Souri M, et al. (1997). "D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder.". Am. J. Hum. Genet. 61 (5): 1153–62. PMID 9345094.
van Grunsven EG, van Berkel E, Ijlst L, et al. (1998). "Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency.". Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2128–33. PMID 9482850.
Dong Y, Qiu QQ, Debear J, et al. (1999). "17Beta-hydroxysteroid dehydrogenases in human bone cells.". J. Bone Miner. Res. 13 (10): 1539–46. PMID 9783542.
Leenders F, Dolez V, Begue A, et al. (1999). "Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV.". Mamm. Genome 9 (12): 1036–41. PMID 9880674.
Green VL, Speirs V, Landolt AM, et al. (1999). "17Beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary adenomas.". J. Clin. Endocrinol. Metab. 84 (4): 1340–5. PMID 10199776.
van Grunsven EG, Mooijer PA, Aubourg P, Wanders RJ (1999). "Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency.". Hum. Mol. Genet. 8 (8): 1509–16. PMID 10400999.
Itoh M, Suzuki Y, Takashima S (1999). "A novel peroxisomal enzyme, D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein: its expression in the developing human brain.". Microsc. Res. Tech. 45 (6): 383–8. doi:10.1002/(SICI)1097-0029(19990615)45:6<383::AID-JEMT5>3.0.CO;2-7. PMID 10402265.
Möller G, Leenders F, van Grunsven EG, et al. (1999). "Characterization of the HSD17B4 gene: D-specific multifunctional protein 2/17beta-hydroxysteroid dehydrogenase IV.". J. Steroid Biochem. Mol. Biol. 69 (1-6): 441–6. PMID 10419023.
Haapalainen AM, van Aalten DM, Meriläinen G, et al. (2001). "Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution.". J. Mol. Biol. 313 (5): 1127–38. doi:10.1006/jmbi.2001.5084. PMID 11700068.