HSD17B4: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Bot: HTTP→HTTPS)
imported>Boghog
(removed no longer needed PBB controls and templates; consistent citation formatting)
 
Line 1: Line 1:
{{Infobox gene}}
{{Infobox gene}}


'''D-bifunctional protein''' ('''DBP'''), also known as '''peroxisomal multifunctional enzyme type 2''' ('''MFP-2'''), as well as '''17β-hydroxysteroid dehydrogenase type IV''' ('''17β-HSD type IV''') is a [[protein]] that in humans is encoded by the ''HSD17B4'' [[gene]].<ref name="pmid8938456">{{cite journal |vauthors=Leenders F, Prescher G, Dolez V, Begue A, de Launoit Y, Adamski J | title = Assignment of human 17 beta-hydroxysteroid dehydrogenase IV to chromosome 5q2 by fluorescence in situ hybridization | journal = Genomics | volume = 37 | issue = 3 | pages = 403–4 |date=Mar 1997 | pmid = 8938456 | pmc =  | doi =10.1006/geno.1996.0578 }}</ref><ref name="pmid19027726">{{cite journal |vauthors=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 |date=Feb 2009 | pmid = 19027726 | pmc = 2896744| doi = 10.1016/j.cbi.2008.10.040 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3295| accessdate = }}</ref><ref name="pmid16766224">{{cite journal | vauthors = Huyghe S, Mannaerts GP, Baes M, Van Veldhoven PP | title = Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model | journal = Biochim. Biophys. Acta | volume = 1761 | issue = 9 | pages = 973–94 | year = 2006 | pmid = 16766224 | doi = 10.1016/j.bbalip.2006.04.006 | url = }}</ref> It is involved in [[fatty acid]] [[beta oxidation|β-oxidation]] and [[steroid]] [[metabolism]].<ref name="pmid16766224" />
'''D-bifunctional protein''' ('''DBP'''), also known as '''peroxisomal multifunctional enzyme type 2''' ('''MFP-2'''), as well as '''17β-hydroxysteroid dehydrogenase type IV''' ('''17β-HSD type IV''') is a [[protein]] that in humans is encoded by the ''HSD17B4'' [[gene]].<ref name="pmid8938456">{{cite journal | vauthors = Leenders F, Prescher G, Dolez V, Begue A, de Launoit Y, Adamski J | title = Assignment of human 17 beta-hydroxysteroid dehydrogenase IV to chromosome 5q2 by fluorescence in situ hybridization | journal = Genomics | volume = 37 | issue = 3 | pages = 403–4 | date = November 1996 | pmid = 8938456 | pmc =  | doi = 10.1006/geno.1996.0578 }}</ref><ref name="pmid19027726">{{cite journal | vauthors = Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall 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 = Chemico-Biological Interactions | volume = 178 | issue = 1-3 | pages = 94–8 | date = March 2009 | pmid = 19027726 | pmc = 2896744 | doi = 10.1016/j.cbi.2008.10.040 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3295| access-date = }}</ref><ref name="pmid16766224">{{cite journal | vauthors = Huyghe S, Mannaerts GP, Baes M, Van Veldhoven PP | title = Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model | journal = Biochimica et Biophysica Acta | volume = 1761 | issue = 9 | pages = 973–94 | date = September 2006 | pmid = 16766224 | doi = 10.1016/j.bbalip.2006.04.006 }}</ref> It's an [[alcohol oxidoreductase]], specifically [[17β-Hydroxysteroid dehydrogenase]]. It is involved in [[fatty acid]] [[beta oxidation|β-oxidation]] and [[steroid]] [[metabolism]] (cf. [[steroidogenesis]]).<ref name="pmid16766224" />


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{PBB_Summary
| section_title =  
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3295| accessdate = }}</ref>
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==
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]<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3295| access-date = }}</ref>
 
== See also ==
* [[D-bifunctional protein deficiency]]
* [[D-bifunctional protein deficiency]]
* [[Perrault syndrome]]
* [[Perrault syndrome]]


==References==
== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = de Launoit Y, Adamski J | title = Unique multifunctional HSD17B4 gene product: 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome | journal = Journal of Molecular Endocrinology | volume = 22 | issue = 3 | pages = 227–40 | date = June 1999 | pmid = 10343282 | doi = 10.1677/jme.0.0220227 }}
| citations =
* {{cite journal | vauthors = Huyghe S, Mannaerts GP, Baes M, Van Veldhoven PP | title = Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model | journal = Biochimica et Biophysica Acta | volume = 1761 | issue = 9 | pages = 973–94 | date = September 2006 | pmid = 16766224 | doi = 10.1016/j.bbalip.2006.04.006 }}
*{{cite journal |vauthors=de Launoit Y, Adamski J |title=Unique multifunctional HSD17B4 gene product: 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome. |journal=J. Mol. Endocrinol. |volume=22 |issue= 3 |pages= 227–40 |year= 1999 |pmid= 10343282 |doi=10.1677/jme.0.0220227 }}
* {{cite journal | vauthors = Palosaari PM, Hiltunen JK | title = 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 | journal = The Journal of Biological Chemistry | volume = 265 | issue = 5 | pages = 2446–9 | date = February 1990 | pmid = 2303409 | doi =  }}
*{{cite journal |vauthors=Huyghe S, Mannaerts GP, Baes M, Van Veldhoven PP |title=Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model. |journal=Biochim. Biophys. Acta |volume=1761 |issue= 9 |pages= 973–94 |year= 2006 |pmid= 16766224 |doi= 10.1016/j.bbalip.2006.04.006 }}
* {{cite journal | vauthors = Adamski J, Normand T, Leenders F, Monté D, Begue A, Stéhelin D, Jungblut PW, de Launoit Y | title = Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV | journal = The Biochemical Journal | volume = 311 ( Pt 2) | issue = 2 | pages = 437–43 | date = October 1995 | pmid = 7487879 | pmc = 1136019 | doi =  }}
*{{cite journal |vauthors=Palosaari PM, Hiltunen JK |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2446–9 |year= 1990 |pmid= 2303409 |doi=  }}
* {{cite journal | vauthors = Markus M, Husen B, Adamski J | title = The subcellular localization of 17 beta-hydroxysteroid dehydrogenase type 4 and its interaction with actin | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 55 | issue = 5-6 | pages = 617–21 | date = December 1995 | pmid = 8547189 | doi = 10.1016/0960-0760(95)00213-8 }}
*{{cite journal   |vauthors=Adamski J, Normand T, Leenders F, etal |title=Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV. |journal=Biochem. J. |volume=311 |issue= 2|pages= 437–43 |year= 1995 |pmid= 7487879 |doi= | pmc=1136019 }}
* {{cite journal | vauthors = Jiang LL, Kobayashi A, Matsuura H, Fukushima H, Hashimoto T | title = Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase | journal = Journal of Biochemistry | volume = 120 | issue = 3 | pages = 624–32 | date = September 1996 | pmid = 8902629 | doi = 10.1093/oxfordjournals.jbchem.a021458 }}
*{{cite journal |vauthors=Markus M, Husen B, Adamski J |title=The subcellular localization of 17 beta-hydroxysteroid dehydrogenase type 4 and its interaction with actin. |journal=J. Steroid Biochem. Mol. Biol. |volume=55 |issue= 5-6 |pages= 617–21 |year= 1996 |pmid= 8547189 |doi=10.1016/0960-0760(95)00213-8 }}
* {{cite journal | vauthors = Jiang LL, Miyazawa S, Souri M, Hashimoto T | title = Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein | journal = Journal of Biochemistry | volume = 121 | issue = 2 | pages = 364–9 | date = February 1997 | pmid = 9089413 | doi = 10.1093/oxfordjournals.jbchem.a021596 }}
*{{cite journal   |vauthors=Jiang LL, Kobayashi A, Matsuura H, etal |title=Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. |journal=J. Biochem. |volume=120 |issue= 3 |pages= 624–32 |year= 1997 |pmid= 8902629 |doi= 10.1093/oxfordjournals.jbchem.a021458}}
* {{cite journal | vauthors = Jiang LL, Kurosawa T, Sato M, Suzuki Y, Hashimoto T | title = Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein | journal = Journal of Biochemistry | volume = 121 | issue = 3 | pages = 506–13 | date = March 1997 | pmid = 9133619 | doi = 10.1093/oxfordjournals.jbchem.a021615 }}
*{{cite journal |vauthors=Jiang LL, Miyazawa S, Souri M, Hashimoto T |title=Structure of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. |journal=J. Biochem. |volume=121 |issue= 2 |pages= 364–9 |year= 1997 |pmid= 9089413 |doi= 10.1093/oxfordjournals.jbchem.a021596}}
* {{cite journal | vauthors = Novikov D, Dieuaide-Noubhani M, Vermeesch JR, Fournier B, Mannaerts GP, Van Veldhoven PP | title = The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping | journal = Biochimica et Biophysica Acta | volume = 1360 | issue = 3 | pages = 229–40 | date = May 1997 | pmid = 9197465 | doi = 10.1016/s0925-4439(97)00003-3 }}
*{{cite journal   |vauthors=Jiang LL, Kurosawa T, Sato M, etal |title=Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. |journal=J. Biochem. |volume=121 |issue= 3 |pages= 506–13 |year= 1997 |pmid= 9133619 |doi= 10.1093/oxfordjournals.jbchem.a021615}}
* {{cite journal | vauthors = Suzuki Y, Jiang LL, Souri M, Miyazawa S, Fukuda S, Zhang Z, Une M, Shimozawa N, Kondo N, Orii T, Hashimoto T | title = D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder | journal = American Journal of Human Genetics | volume = 61 | issue = 5 | pages = 1153–62 | date = November 1997 | pmid = 9345094 | pmc = 1716023 | doi = 10.1086/301599 }}
*{{cite journal   |vauthors=Novikov D, Dieuaide-Noubhani M, Vermeesch JR, etal |title=The human peroxisomal multifunctional protein involved in bile acid synthesis: activity measurement, deficiency in Zellweger syndrome and chromosome mapping. |journal=Biochim. Biophys. Acta |volume=1360 |issue= 3 |pages= 229–40 |year= 1997 |pmid= 9197465 |doi= 10.1016/s0925-4439(97)00003-3}}
* {{cite journal | vauthors = van Grunsven EG, van Berkel E, Ijlst L, Vreken P, de Klerk JB, Adamski J, Lemonde H, Clayton PT, Cuebas DA, Wanders RJ | title = Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 5 | pages = 2128–33 | date = March 1998 | pmid = 9482850 | pmc = 19272 | doi = 10.1073/pnas.95.5.2128 }}
*{{cite journal   |vauthors=Suzuki Y, Jiang LL, Souri M, etal |title=D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein deficiency: a newly identified peroxisomal disorder. |journal=Am. J. Hum. Genet. |volume=61 |issue= 5 |pages= 1153–62 |year= 1997 |pmid= 9345094 |doi=10.1086/301599 | pmc=1716023  }}
* {{cite journal | vauthors = Dong Y, Qiu QQ, Debear J, Lathrop WF, Bertolini DR, Tamburini PP | title = 17Beta-hydroxysteroid dehydrogenases in human bone cells | journal = Journal of Bone and Mineral Research | volume = 13 | issue = 10 | pages = 1539–46 | date = October 1998 | pmid = 9783542 | doi = 10.1359/jbmr.1998.13.10.1539 }}
*{{cite journal   |vauthors=van Grunsven EG, van Berkel E, IJlst L, etal |title=Peroxisomal D-hydroxyacyl-CoA dehydrogenase deficiency: resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 5 |pages= 2128–33 |year= 1998 |pmid= 9482850 |doi=10.1073/pnas.95.5.2128 | pmc=19272  }}
* {{cite journal | vauthors = Leenders F, Dolez V, Begue A, Möller G, Gloeckner JC, de Launoit Y, Adamski J | title = Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV | journal = Mammalian Genome | volume = 9 | issue = 12 | pages = 1036–41 | date = December 1998 | pmid = 9880674 | doi = 10.1007/s003359900921 }}
*{{cite journal   |vauthors=Dong Y, Qiu QQ, Debear J, etal |title=17Beta-hydroxysteroid dehydrogenases in human bone cells. |journal=J. Bone Miner. Res. |volume=13 |issue= 10 |pages= 1539–46 |year= 1999 |pmid= 9783542 |doi=10.1359/jbmr.1998.13.10.1539 }}
* {{cite journal | vauthors = Green VL, Speirs V, Landolt AM, Foy PM, Atkin SL | title = 17Beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary adenomas | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 84 | issue = 4 | pages = 1340–5 | date = April 1999 | pmid = 10199776 | doi = 10.1210/jc.84.4.1340 | author-link2 = Valerie Speirs }}
*{{cite journal   |vauthors=Leenders F, Dolez V, Begue A, etal |title=Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV. |journal=Mamm. Genome |volume=9 |issue= 12 |pages= 1036–41 |year= 1999 |pmid= 9880674 |doi=10.1007/s003359900921 }}
* {{cite journal | vauthors = van Grunsven EG, Mooijer PA, Aubourg P, Wanders RJ | title = Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency | journal = Human Molecular Genetics | volume = 8 | issue = 8 | pages = 1509–16 | date = August 1999 | pmid = 10400999 | doi = 10.1093/hmg/8.8.1509 }}
*{{cite journal   |vauthors=Green VL, Speirs V, Landolt AM, etal |title=17Beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 expression and enzyme activity in human anterior pituitary adenomas. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 4 |pages= 1340–5 |year= 1999 |pmid= 10199776 |doi=10.1210/jc.84.4.1340 }}
* {{cite journal | vauthors = Itoh M, Suzuki Y, Takashima S | title = A novel peroxisomal enzyme, D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein: its expression in the developing human brain | journal = Microscopy Research and Technique | volume = 45 | issue = 6 | pages = 383–8 | date = June 1999 | pmid = 10402265 | doi = 10.1002/(SICI)1097-0029(19990615)45:6<383::AID-JEMT5>3.0.CO;2-7 }}
*{{cite journal |vauthors=van Grunsven EG, Mooijer PA, Aubourg P, Wanders RJ |title=Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency. |journal=Hum. Mol. Genet. |volume=8 |issue= 8 |pages= 1509–16 |year= 1999 |pmid= 10400999 |doi=10.1093/hmg/8.8.1509 }}
* {{cite journal | vauthors = Möller G, Leenders F, van Grunsven EG, Dolez V, Qualmann B, Kessels MM, Markus M, Krazeisen A, Husen B, Wanders RJ, de Launoit Y, Adamski J | title = Characterization of the HSD17B4 gene: D-specific multifunctional protein 2/17beta-hydroxysteroid dehydrogenase IV | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 69 | issue = 1-6 | pages = 441–6 | year = 1999 | pmid = 10419023 | doi = 10.1016/S0960-0760(99)00066-7 }}
*{{cite journal |vauthors=Itoh M, Suzuki Y, Takashima S |title=A novel peroxisomal enzyme, D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein: its expression in the developing human brain. |journal=Microsc. Res. Tech. |volume=45 |issue= 6 |pages= 383–8 |year= 1999 |pmid= 10402265 |doi= 10.1002/(SICI)1097-0029(19990615)45:6<383::AID-JEMT5>3.0.CO;2-7 }}
* {{cite journal | vauthors = Haapalainen AM, van Aalten DM, Meriläinen G, Jalonen JE, Pirilä P, Wierenga RK, Hiltunen JK, Glumoff T | title = Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution | journal = Journal of Molecular Biology | volume = 313 | issue = 5 | pages = 1127–38 | date = November 2001 | pmid = 11700068 | doi = 10.1006/jmbi.2001.5084 }}
*{{cite journal   |vauthors=Möller G, Leenders F, van Grunsven EG, etal |title=Characterization of the HSD17B4 gene: D-specific multifunctional protein 2/17beta-hydroxysteroid dehydrogenase IV. |journal=J. Steroid Biochem. Mol. Biol. |volume=69 |issue= 1-6 |pages= 441–6 |year= 1999 |pmid= 10419023 |doi=10.1016/S0960-0760(99)00066-7 }}
*{{cite journal   |vauthors=Haapalainen AM, van Aalten DM, Meriläinen G, etal |title=Crystal structure of the liganded SCP-2-like domain of human peroxisomal multifunctional enzyme type 2 at 1.75 A resolution. |journal=J. Mol. Biol. |volume=313 |issue= 5 |pages= 1127–38 |year= 2001 |pmid= 11700068 |doi= 10.1006/jmbi.2001.5084 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3295}}
{{PDB Gallery|geneid=3295}}


<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
{{Peroxisomal metabolism enzymes}}
{{Peroxisomal metabolism enzymes}}


{{gene-5-stub}}
{{gene-5-stub}}

Latest revision as of 08:53, 6 November 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

D-bifunctional protein (DBP), also known as peroxisomal multifunctional enzyme type 2 (MFP-2), as well as 17β-hydroxysteroid dehydrogenase type IV (17β-HSD type IV) is a protein that in humans is encoded by the HSD17B4 gene.[1][2][3][4] It's an alcohol oxidoreductase, specifically 17β-Hydroxysteroid dehydrogenase. It is involved in fatty acid β-oxidation and steroid metabolism (cf. steroidogenesis).[4]

Function

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][3]

See also

References

  1. ↑ Leenders F, Prescher G, Dolez V, Begue A, de Launoit Y, Adamski J (November 1996). "Assignment of human 17 beta-hydroxysteroid dehydrogenase IV to chromosome 5q2 by fluorescence in situ hybridization". Genomics. 37 (3): 403–4. doi:10.1006/geno.1996.0578. PMID 8938456.
  2. ↑ Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (March 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1–3): 94–8. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
  3. ↑ 3.0 3.1 "Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4".
  4. ↑ 4.0 4.1 Huyghe S, Mannaerts GP, Baes M, Van Veldhoven PP (September 2006). "Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model". Biochimica et Biophysica Acta. 1761 (9): 973–94. doi:10.1016/j.bbalip.2006.04.006. PMID 16766224.

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=HSD17B4&oldid=1532900"