HADHA: Difference between revisions
Jump to navigation
Jump to search
m Bot: HTTP→HTTPS |
imported>John of Reading m →Structure: Typo fixing, replaced: a 82.9 → an 82.9 |
||
| Line 1: | Line 1: | ||
{{Infobox_gene}} | {{Infobox_gene}} | ||
'''Trifunctional enzyme subunit alpha, mitochondrial''' also known as '''hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit''' is a [[protein]] that in humans is encoded by the HADHA [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit | '''Trifunctional enzyme subunit alpha, mitochondrial''' also known as '''hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit''' is a [[protein]] that in humans is encoded by the ''HADHA'' [[gene]]. Mutations in ''HADHA'' have been associated with [[Mitochondrial trifunctional protein deficiency|trifunctional protein deficiency]] or [[long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency]].<ref name="entrez">{{cite web|url=https://www.ncbi.nlm.nih.gov/gene/3030|title=Entrez Gene: Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit}}</ref> | ||
==Structure== | ==Structure== | ||
HADHA is | HADHA is an 82.9 kDa protein composed of 763 amino acids.<ref name=COPaKB>{{cite journal | vauthors = Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P | title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase | journal = Circulation Research | volume = 113 | issue = 9 | pages = 1043–53 | date = Oct 2013 | pmid = 23965338 | pmc = 4076475 | doi = 10.1161/CIRCRESAHA.113.301151 }}</ref><ref name="url_COPaKB">{{cite web | url = http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P40939 | work = Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) | title = hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit }}</ref> | ||
The [[mitochondrial]] membrane-bound heterocomplex is composed of four alpha and four beta subunits, with the alpha subunit catalyzing the [[3-hydroxyacyl-CoA dehydrogenase]] and [[enoyl-CoA hydratase]] activities. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation.<ref name="entrez"/> | The [[mitochondrial]] membrane-bound heterocomplex is composed of four alpha and four beta subunits, with the alpha subunit catalyzing the [[3-hydroxyacyl-CoA dehydrogenase]] and [[enoyl-CoA hydratase]] activities. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation.<ref name="entrez"/> | ||
| Line 10: | Line 10: | ||
== Function == | == Function == | ||
This gene encodes the alpha subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids.<ref name="entrez"/> The enzyme converts medium- and long-chain 2-enoyl-CoA compounds into the following 3-ketoacyl-CoA when NAD is solely present, and acetyl-CoA when NAD and CoASH are present.<ref>{{cite journal | vauthors = Carpenter K, Pollitt RJ, Middleton B | title = Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria | journal = Biochemical and Biophysical Research Communications | volume = 183 | issue = 2 | pages = 443–8 | date = Mar 1992 | pmid = 1550553 | doi=10.1016/0006-291x(92)90501-b}}</ref> The alpha subunit catalyzes this reaction, and is attached to HADHB, which catalyzes the last step of the reaction.<ref name="BioChem">{{cite book | title = Principles of Biochemistry | chapter = Chapter 18, Mitochondrial ATP synthesis | first1 = Donald J. | last1 = Voet | first2 = Judith G. | last2 = Voet | first3 = Charlotte W. | last3 = Pratt | publisher = Wiley | year = 2010 | isbn = 978-0-470-23396-2 | page = 669 | edition = 4th | name-list-format = vanc }}</ref> | This gene encodes the alpha subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial [[Beta oxidation|beta-oxidation]] of long chain fatty acids.<ref name="entrez"/> The enzyme converts medium- and long-chain 2-enoyl-CoA compounds into the following 3-ketoacyl-CoA when NAD is solely present, and [[acetyl-CoA]] when NAD and [[CoASH]] are present.<ref>{{cite journal | vauthors = Carpenter K, Pollitt RJ, Middleton B | title = Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria | journal = Biochemical and Biophysical Research Communications | volume = 183 | issue = 2 | pages = 443–8 | date = Mar 1992 | pmid = 1550553 | doi=10.1016/0006-291x(92)90501-b}}</ref> The alpha subunit catalyzes this reaction, and is attached to [[HADHB]], which catalyzes the last step of the reaction.<ref name="BioChem">{{cite book | title = Principles of Biochemistry | chapter = Chapter 18, Mitochondrial ATP synthesis | first1 = Donald J. | last1 = Voet | first2 = Judith G. | last2 = Voet | first3 = Charlotte W. | last3 = Pratt | publisher = Wiley | year = 2010 | isbn = 978-0-470-23396-2 | page = 669 | edition = 4th | name-list-format = vanc }}</ref> | ||
== Clinical significance == | == Clinical significance == | ||
Mutations in this gene result in trifunctional protein deficiency or [[long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency]].<ref name="entrez"/> | Mutations in this gene result in trifunctional protein deficiency or [[long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency]].<ref name="entrez"/> | ||
The most common form of the mutation is G1528C, in which the guanine at the 1528th position is changed to a cytosine. The gene mutation creates a protein deficiency that is associated with impaired oxidation of long-chain fatty acids that can lead to sudden infant death.<ref>{{cite journal | vauthors = IJlst L, Ruiter JP, Hoovers JM, Jakobs ME, Wanders RJ | title = Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene | journal = The Journal of Clinical Investigation | volume = 98 | issue = 4 | pages = 1028–33 | date = | The most common form of the mutation is G1528C, in which the [[guanine]] at the 1528th position is changed to a [[cytosine]]. The gene mutation creates a protein deficiency that is associated with impaired oxidation of [[Fatty acid|long-chain fatty acids]] that can lead to sudden infant death.<ref>{{cite journal | vauthors = IJlst L, Ruiter JP, Hoovers JM, Jakobs ME, Wanders RJ | title = Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene | journal = The Journal of Clinical Investigation | volume = 98 | issue = 4 | pages = 1028–33 | date = August 1996 | pmid = 8770876 | pmc = 507519 | doi = 10.1172/jci118863 }}</ref> Clinical manifestations of this deficiency can include [[myopathy]], [[cardiomyopathy]], episodes of [[coma]], and [[hypoglycemia]].<ref>{{cite journal | vauthors = Rocchiccioli F, Wanders RJ, Aubourg P, Vianey-Liaud C, Ijlst L, Fabre M, Cartier N, Bougneres PF | title = Deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase: a cause of lethal myopathy and cardiomyopathy in early childhood | journal = Pediatric Research | volume = 28 | issue = 6 | pages = 657–62 | date = December 1990 | pmid = 2284166 | doi = 10.1203/00006450-199012000-00023 }}</ref> Long-chain L-3-hydroxyacyl-coenzyme A dehydrogenase deficiency is associated with some pregnancy-specific disorders, including [[Pre-eclampsia|preeclampsia]], [[HELLP syndrome]] (hemolysis, elevated liver enzymes, low platelets), [[hyperemesis gravidarum]], acute fatty liver of pregnancy, and maternal floor infarct of the placenta.<ref>{{cite journal | vauthors = Rakheja D, Bennett MJ, Rogers BB | title = Long-chain L-3-hydroxyacyl-coenzyme a dehydrogenase deficiency: a molecular and biochemical review | journal = Laboratory Investigation; A Journal of Technical Methods and Pathology | volume = 82 | issue = 7 | pages = 815–24 | date = July 2002 | pmid = 12118083 | doi = 10.1097/01.lab.0000021175.50201.46 }}</ref><ref>{{cite journal | vauthors = Griffin AC, Strauss AW, Bennett MJ, Ernst LM | title = Mutations in long-chain 3-hydroxyacyl coenzyme a dehydrogenase are associated with placental maternal floor infarction/massive perivillous fibrin deposition | journal = Pediatric and Developmental Pathology | volume = 15 | issue = 5 | pages = 368–74 | date = September–October 2012 | pmid = 22746996 | doi = 10.2350/12-05-1198-oa.1 }}</ref> Additionally, it has been correlated with [[Acute fatty liver of pregnancy]] (AFLP) disease.<ref>{{cite journal | vauthors = Ibdah JA, Yang Z, Bennett MJ | title = Liver disease in pregnancy and fetal fatty acid oxidation defects | journal = Molecular Genetics and Metabolism | volume = 71 | issue = 1–2 | pages = 182–9 | date = September–October 2000 | pmid = 11001809 | doi = 10.1006/mgme.2000.3065 }}</ref> | ||
From a clinical perspective, HADHA might also be a useful marker to predict resistance to certain types of chemotherapy in patients with lung cancer.<ref>{{cite journal | vauthors = Kageyama T, Nagashio R, Ryuge S, Matsumoto T, Iyoda A, Satoh Y, Masuda N, Jiang SX, Saegusa M, Sato Y | title = HADHA is a potential predictor of response to platinum-based chemotherapy for lung cancer | journal = Asian Pacific Journal of Cancer Prevention | volume = 12 | issue = 12 | pages = 3457–63 | date = 2011 | pmid = 22471497 }}</ref> | From a clinical perspective, HADHA might also be a useful marker to predict resistance to certain types of [[chemotherapy]] in patients with [[lung cancer]].<ref>{{cite journal | vauthors = Kageyama T, Nagashio R, Ryuge S, Matsumoto T, Iyoda A, Satoh Y, Masuda N, Jiang SX, Saegusa M, Sato Y | title = HADHA is a potential predictor of response to platinum-based chemotherapy for lung cancer | journal = Asian Pacific Journal of Cancer Prevention | volume = 12 | issue = 12 | pages = 3457–63 | date = 2011 | pmid = 22471497 }}</ref> | ||
== Interactions == | |||
HADHA has been shown to have 142 binary [[Protein–protein interaction|protein-protein interactions]] including 117 co-complex interactions. HADHA appears to interact with [[GABARAP]], [[MAP1LC3B]], [[TRAF6]], [[GABARAPL2]], GABARAPL1, GAST, [[BCAR3]], [[EPB41]], [[TNFRSF1A]], [[HLA-B]], [[NFKB2]], [[MAP3K1]], [[IKBKE]], [[PRKAB1]], [[RIPK3]], [[CD74]], [[NR4A1]], cdsA, mtaD, [[ATXN2L]], [[ABCF2]], and [[MAPK3]].<ref>{{Cite web | url = https://www.ebi.ac.uk/intact/interactions?conversationContext=3&query=HADHA | title = 142 binary interactions found for search term HADHA | work = IntAct Molecular Interaction Database | publisher = EMBL-EBI | access-date = 2018-08-25 }}</ref> | |||
== References == | == References == | ||
{{reflist| | {{reflist|32em}} | ||
== Further reading == | == Further reading == | ||
{{refbegin| | {{refbegin|32em}} | ||
* {{cite journal | vauthors = Rakheja D, Bennett MJ, Rogers BB | title = Long-chain L-3-hydroxyacyl-coenzyme a dehydrogenase deficiency: a molecular and biochemical review | journal = Laboratory Investigation | volume = 82 | issue = 7 | date = Jul 2002 | pmid = 12118083 | doi=10.1097/01.lab.0000021175.50201.46 | pages=815–24}} | * {{cite journal | vauthors = Rakheja D, Bennett MJ, Rogers BB | title = Long-chain L-3-hydroxyacyl-coenzyme a dehydrogenase deficiency: a molecular and biochemical review | journal = Laboratory Investigation | volume = 82 | issue = 7 | date = Jul 2002 | pmid = 12118083 | doi=10.1097/01.lab.0000021175.50201.46 | pages=815–24}} | ||
* {{cite journal | vauthors = Isaacs JD, Sims HF, Powell CK, Bennett MJ, Hale DE, Treem WR, Strauss AW | title = Maternal acute fatty liver of pregnancy associated with fetal trifunctional protein deficiency: molecular characterization of a novel maternal mutant allele | journal = Pediatric Research | volume = 40 | issue = 3 | date = Sep 1996 | pmid = 8865274 | doi = 10.1203/00006450-199609000-00005 | pages=393–8}} | * {{cite journal | vauthors = Isaacs JD, Sims HF, Powell CK, Bennett MJ, Hale DE, Treem WR, Strauss AW | title = Maternal acute fatty liver of pregnancy associated with fetal trifunctional protein deficiency: molecular characterization of a novel maternal mutant allele | journal = Pediatric Research | volume = 40 | issue = 3 | date = Sep 1996 | pmid = 8865274 | doi = 10.1203/00006450-199609000-00005 | pages=393–8}} | ||
Latest revision as of 16:31, 14 December 2018
| VALUE_ERROR (nil) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Aliases | |||||||
| External IDs | GeneCards: [1] | ||||||
| Orthologs | |||||||
| Species | Human | Mouse | |||||
| Entrez |
|
| |||||
| Ensembl |
|
| |||||
| UniProt |
|
| |||||
| RefSeq (mRNA) |
|
| |||||
| RefSeq (protein) |
|
| |||||
| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
| Wikidata | |||||||
| |||||||
Trifunctional enzyme subunit alpha, mitochondrial also known as hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit is a protein that in humans is encoded by the HADHA gene. Mutations in HADHA have been associated with trifunctional protein deficiency or long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency.[1]
Structure
HADHA is an 82.9 kDa protein composed of 763 amino acids.[2][3]
The mitochondrial membrane-bound heterocomplex is composed of four alpha and four beta subunits, with the alpha subunit catalyzing the 3-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase activities. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation.[1]
Function
This gene encodes the alpha subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids.[1] The enzyme converts medium- and long-chain 2-enoyl-CoA compounds into the following 3-ketoacyl-CoA when NAD is solely present, and acetyl-CoA when NAD and CoASH are present.[4] The alpha subunit catalyzes this reaction, and is attached to HADHB, which catalyzes the last step of the reaction.[5]
Clinical significance
Mutations in this gene result in trifunctional protein deficiency or long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency.[1]
The most common form of the mutation is G1528C, in which the guanine at the 1528th position is changed to a cytosine. The gene mutation creates a protein deficiency that is associated with impaired oxidation of long-chain fatty acids that can lead to sudden infant death.[6] Clinical manifestations of this deficiency can include myopathy, cardiomyopathy, episodes of coma, and hypoglycemia.[7] Long-chain L-3-hydroxyacyl-coenzyme A dehydrogenase deficiency is associated with some pregnancy-specific disorders, including preeclampsia, HELLP syndrome (hemolysis, elevated liver enzymes, low platelets), hyperemesis gravidarum, acute fatty liver of pregnancy, and maternal floor infarct of the placenta.[8][9] Additionally, it has been correlated with Acute fatty liver of pregnancy (AFLP) disease.[10]
From a clinical perspective, HADHA might also be a useful marker to predict resistance to certain types of chemotherapy in patients with lung cancer.[11]
Interactions
HADHA has been shown to have 142 binary protein-protein interactions including 117 co-complex interactions. HADHA appears to interact with GABARAP, MAP1LC3B, TRAF6, GABARAPL2, GABARAPL1, GAST, BCAR3, EPB41, TNFRSF1A, HLA-B, NFKB2, MAP3K1, IKBKE, PRKAB1, RIPK3, CD74, NR4A1, cdsA, mtaD, ATXN2L, ABCF2, and MAPK3.[12]
References
- ↑ 1.0 1.1 1.2 1.3 "Entrez Gene: Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit".
- ↑ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
- ↑ "hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), alpha subunit". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).
- ↑ Carpenter K, Pollitt RJ, Middleton B (Mar 1992). "Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria". Biochemical and Biophysical Research Communications. 183 (2): 443–8. doi:10.1016/0006-291x(92)90501-b. PMID 1550553.
- ↑ Voet DJ, Voet JG, Pratt CW (2010). "Chapter 18, Mitochondrial ATP synthesis". Principles of Biochemistry (4th ed.). Wiley. p. 669. ISBN 978-0-470-23396-2.
- ↑ IJlst L, Ruiter JP, Hoovers JM, Jakobs ME, Wanders RJ (August 1996). "Common missense mutation G1528C in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Characterization and expression of the mutant protein, mutation analysis on genomic DNA and chromosomal localization of the mitochondrial trifunctional protein alpha subunit gene". The Journal of Clinical Investigation. 98 (4): 1028–33. doi:10.1172/jci118863. PMC 507519. PMID 8770876.
- ↑ Rocchiccioli F, Wanders RJ, Aubourg P, Vianey-Liaud C, Ijlst L, Fabre M, Cartier N, Bougneres PF (December 1990). "Deficiency of long-chain 3-hydroxyacyl-CoA dehydrogenase: a cause of lethal myopathy and cardiomyopathy in early childhood". Pediatric Research. 28 (6): 657–62. doi:10.1203/00006450-199012000-00023. PMID 2284166.
- ↑ Rakheja D, Bennett MJ, Rogers BB (July 2002). "Long-chain L-3-hydroxyacyl-coenzyme a dehydrogenase deficiency: a molecular and biochemical review". Laboratory Investigation; A Journal of Technical Methods and Pathology. 82 (7): 815–24. doi:10.1097/01.lab.0000021175.50201.46. PMID 12118083.
- ↑ Griffin AC, Strauss AW, Bennett MJ, Ernst LM (September–October 2012). "Mutations in long-chain 3-hydroxyacyl coenzyme a dehydrogenase are associated with placental maternal floor infarction/massive perivillous fibrin deposition". Pediatric and Developmental Pathology. 15 (5): 368–74. doi:10.2350/12-05-1198-oa.1. PMID 22746996.
- ↑ Ibdah JA, Yang Z, Bennett MJ (September–October 2000). "Liver disease in pregnancy and fetal fatty acid oxidation defects". Molecular Genetics and Metabolism. 71 (1–2): 182–9. doi:10.1006/mgme.2000.3065. PMID 11001809.
- ↑ Kageyama T, Nagashio R, Ryuge S, Matsumoto T, Iyoda A, Satoh Y, Masuda N, Jiang SX, Saegusa M, Sato Y (2011). "HADHA is a potential predictor of response to platinum-based chemotherapy for lung cancer". Asian Pacific Journal of Cancer Prevention. 12 (12): 3457–63. PMID 22471497.
- ↑ "142 binary interactions found for search term HADHA". IntAct Molecular Interaction Database. EMBL-EBI. Retrieved 2018-08-25.
Further reading
- Rakheja D, Bennett MJ, Rogers BB (Jul 2002). "Long-chain L-3-hydroxyacyl-coenzyme a dehydrogenase deficiency: a molecular and biochemical review". Laboratory Investigation. 82 (7): 815–24. doi:10.1097/01.lab.0000021175.50201.46. PMID 12118083.
- Isaacs JD, Sims HF, Powell CK, Bennett MJ, Hale DE, Treem WR, Strauss AW (Sep 1996). "Maternal acute fatty liver of pregnancy associated with fetal trifunctional protein deficiency: molecular characterization of a novel maternal mutant allele". Pediatric Research. 40 (3): 393–8. doi:10.1203/00006450-199609000-00005. PMID 8865274.
- Gillingham MB, Matern D, Harding CO (Oct 2009). "Effect of feeding, exercise and genotype on plasma 3-hydroxyacylcarnitines in children with lchad deficiency". Topics in Clinical Nutrition. 24 (4): 359–365. doi:10.1097/TIN.0b013e3181c62182. PMC 2892921. PMID 20589231.
- Milewska M, McRedmond J, Byrne PC (Nov 2009). "Identification of novel spartin-interactors shows spartin is a multifunctional protein". Journal of Neurochemistry. 111 (4): 1022–30. doi:10.1111/j.1471-4159.2009.06382.x. PMID 19765186.
- Weekes J, Morrison K, Mullen A, Wait R, Barton P, Dunn MJ (Feb 2003). "Hyperubiquitination of proteins in dilated cardiomyopathy". Proteomics. 3 (2): 208–16. doi:10.1002/pmic.200390029. PMID 12601813.
- Bogenhagen DF, Rousseau D, Burke S (Feb 2008). "The layered structure of human mitochondrial DNA nucleoids". Journal of Biological Chemistry. 283 (6): 3665–75. doi:10.1074/jbc.M708444200. PMID 18063578.
- Zhang QX, Baldwin GS (Oct 1994). "Structures of the human cDNA and gene encoding the 78 kDa gastrin-binding protein and of a related pseudogene". Biochimica et Biophysica Acta. 1219 (2): 567–75. doi:10.1016/0167-4781(94)90091-4. PMID 7918661.
- IJlst L, Oostheim W, Ruiter JP, Wanders RJ (Jul 1997). "Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of two new mutations". Journal of Inherited Metabolic Disease. 20 (3): 420–2. doi:10.1023/A:1005310903004. PMID 9266371.
- Yagi M, Lee T, Awano H, Tsuji M, Tajima G, Kobayashi H, Hasegawa Y, Yamaguchi S, Takeshima Y, Matsuo M (Dec 2011). "A patient with mitochondrial trifunctional protein deficiency due to the mutations in the HADHB gene showed recurrent myalgia since early childhood and was diagnosed in adolescence". Molecular Genetics and Metabolism. 104 (4): 556–9. doi:10.1016/j.ymgme.2011.09.025. PMID 22000755.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
 | This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it. |
| Stub icon | This biochemistry article is a stub. You can help Wikipedia by expanding it. |
.svg){kind=link}