HSD17B4: Difference between revisions

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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 is involved in fatty acid β-oxidation and steroid metabolism.^[4]

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]

References

↑ Leenders F, Prescher G, Dolez V, Begue A, de Launoit Y, Adamski J (Mar 1997). "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.
↑ 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. PMC 2896744. PMID 19027726.
↑ ^3.0 ^3.1 "Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4".
↑ ^4.0 ^4.1 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.

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. doi:10.1677/jme.0.0220227. 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 (2): 437–43. PMC 1136019. 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. doi:10.1016/0960-0760(95)00213-8. 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. doi:10.1093/oxfordjournals.jbchem.a021458. PMID 8902629.
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. doi:10.1093/oxfordjournals.jbchem.a021596. 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. doi:10.1093/oxfordjournals.jbchem.a021615. 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. doi:10.1016/s0925-4439(97)00003-3. 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. doi:10.1086/301599. PMC 1716023. 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. doi:10.1073/pnas.95.5.2128. PMC 19272. 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. doi:10.1359/jbmr.1998.13.10.1539. 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. doi:10.1007/s003359900921. 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. doi:10.1210/jc.84.4.1340. 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. doi:10.1093/hmg/8.8.1509. 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. doi:10.1016/S0960-0760(99)00066-7. 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.

This article on a gene on human chromosome 5 is a stub. You can help Wikipedia by expanding it.

[pmid8938456-1] Leenders F, Prescher G, Dolez V, Begue A, de Launoit Y, Adamski J (Mar 1997). "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.

[pmid19027726-2] 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. PMC 2896744. PMID 19027726.

[entrez-3] 3.0 ^3.1 "Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4".

[pmid16766224-4] 4.0 ^4.1 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.

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[3]

[4]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Infobox gene}}
-{{PBB_Controls
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}
-<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+'''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" />
-{{GNF_Protein_box
- | image = PBB_Protein_HSD17B4_image.jpg
- | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ikt.
- | PDB = {{PDB2|1ikt}}, {{PDB2|1s9c}}, {{PDB2|1zbq}}
- | Name = Hydroxysteroid (17-beta) dehydrogenase 4
- | HGNCid = 5213
- | Symbol = HSD17B4
- | AltSymbols =; MFE-2
- | OMIM = 601860
- | ECnumber =
- | Homologene = 358
- | MGIid = 105089
-  | GeneAtlas_image1 = PBB_GE_HSD17B4_201413_at_tn.png
-  | Function = {{GNF_GO|id=GO:0003857 |text = 3-hydroxyacyl-CoA dehydrogenase activity}} {{GNF_GO|id=GO:0004303 |text = estradiol 17-beta-dehydrogenase activity}} {{GNF_GO|id=GO:0005498 |text = sterol carrier activity}} {{GNF_GO|id=GO:0015248 |text = sterol transporter activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
- | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}}
-  | Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 3295
-    | Hs_Ensembl = ENSG00000133835
-    | Hs_RefseqProtein = NP_000405
-    | Hs_RefseqmRNA = NM_000414
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 5
-    | Hs_GenLoc_start = 118816103
-    | Hs_GenLoc_end = 118905926
-    | Hs_Uniprot = P51659
-    | Mm_EntrezGene = 15488
-    | Mm_Ensembl = ENSMUSG00000024507
-    | Mm_RefseqmRNA = NM_008292
-    | Mm_RefseqProtein = NP_032318
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 18
-    | Mm_GenLoc_start = 50253531
-    | Mm_GenLoc_end = 50321514
-    | Mm_Uniprot = Q3TT11
-  }}
-}}
-'''Hydroxysteroid (17-beta) dehydrogenase 4''', also known as '''HSD17B4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B4 hydroxysteroid (17-beta) dehydrogenase 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3295| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{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 = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3295| accessdate = }}</ref>
+| 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>
 }}
+==See also==
+* [[D-bifunctional protein deficiency]]
+* [[Perrault syndrome]]
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=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=  }}
+*{{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  | author=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=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  | author=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=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  | author=Adamski J, Normand T, Leenders F, ''et al.'' |title=Molecular cloning of a novel widely expressed human 80 kDa 17 beta-hydroxysteroid dehydrogenase IV. |journal=Biochem. J. |volume=311 ( Pt 2) |issue=  |pages= 437-43 |year= 1995 |pmid= 7487879 |doi=  }}
+*{{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  | author=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=  }}
+*{{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  | author=Jiang LL, Kobayashi A, Matsuura H, ''et al.'' |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=  }}
+*{{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  | author=Leenders F, Prescher G, Dolez V, ''et al.'' |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 |year= 1997 |pmid= 8938456 |doi=  }}
+*{{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  | author=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=  }}
+*{{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  | author=Jiang LL, Kurosawa T, Sato M, ''et al.'' |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=  }}
+*{{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  | author=Novikov D, Dieuaide-Noubhani M, Vermeesch JR, ''et al.'' |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=  }}
+*{{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  | author=Suzuki Y, Jiang LL, Souri M, ''et al.'' |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=  }}
+*{{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  | author=van Grunsven EG, van Berkel E, Ijlst L, ''et al.'' |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=  }}
+*{{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  | author=Dong Y, Qiu QQ, Debear J, ''et al.'' |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=  }}
+*{{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  | author=Leenders F, Dolez V, Begue A, ''et al.'' |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=  }}
+*{{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  | author=Green VL, Speirs V, Landolt AM, ''et al.'' |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=  }}
+*{{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  | author=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=  }}
+*{{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  | author=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=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  | author=Möller G, Leenders F, van Grunsven EG, ''et al.'' |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=  }}
+*{{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 }}
-*{{cite journal  | author=Haapalainen AM, van Aalten DM, Meriläinen G, ''et al.'' |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}}
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+{{Peroxisomal metabolism enzymes}}
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v t e Peroxisomal and lysosomal proteins
Enzymes	Mevalonate kinase Catalase Acetyl-CoA C-acyltransferase Glyceronephosphate O-acyltransferase Alkylglycerone phosphate synthase Phytanoyl-CoA dioxygenase HSD17B4 AMACR
Transporters	SLC27A2
Structure/Peroxin	PEX1 PXMP3 PEX3 PEX5 PEX6 PEX7 PEX10 PEX11A PEX11B PEX11G PEX12 PEX13 PEX14 PEX16 PEX19 PEX26
LAMP	CD68 LAMP1 LAMP2 LAMP3
see also intermediates, disorders

HSD17B4: Difference between revisions

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