HADHB

Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional protein), beta subunit
Identifiers
Symbols	HADHB; ECHB; MGC87480; MTPB; TP-BETA
External IDs	OMIM: 143450 MGI: 3651143 HomoloGene: 153 GeneCards: HADHB Gene
EC number	2.3.1.16
Gene Ontology Molecular function • fatty-acyl-CoA binding • 3-hydroxyacyl-CoA dehydrogenase activity • acetyl-CoA C-acyltransferase activity • enoyl-CoA hydratase activity • protein binding • acyltransferase activity • long-chain-enoyl-CoA hydratase activity • long-chain-3-hydroxyacyl-CoA dehydrogenase activity • transferase activity • NAD binding Cellular component • mitochondrion • mitochondrial envelope • mitochondrial inner membrane • mitochondrial matrix • fatty acid beta-oxidation multienzyme complex • mitochondrial nucleoid Biological process • fatty acid metabolic process • fatty acid beta-oxidation • cellular lipid metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3032	231086
Ensembl	ENSG00000138029	ENSMUSG00000059447
UniProt	P55084	n/a
RefSeq (mRNA)	NM_000183	NM_145558.1
RefSeq (protein)	NP_000174	NP_663533.1
Location (UCSC)	Chr 2: 26.47 – 26.51 Mb	Chr 5: 30.48 – 30.51 Mb
PubMed search	[1]	[2]

Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, or beta-ketothiolase is an enzyme that in humans is encoded by the HADHB gene.

HADHB is a subunit of the mitochondrial trifunctional protein and has thiolase activity.

Function

This gene encodes the beta subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids. The mitochondrial membrane-bound heterocomplex is composed of four alpha and four beta subunits, with the beta subunit catalyzing the 3-ketoacyl-CoA thiolase activity. Mutations in this gene result in trifunctional protein deficiency. The encoded protein can also bind RNA and decreases the stability of some mRNAs. 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.

Further reading

• Wang R, Yang Z, Zhu JM, et al. (2006). "[Screening for G1528C mutation in mitochondrial trifunctional protein gene in pregnant women with severe preeclampsia and new born infant].". Zhonghua Fu Chan Ke Za Zhi 41 (10): 672–5. PMID 17199921. 
• Aboulaich N, Vainonen JP, StrÃ¥lfors P, Vener AV (2004). "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.". Biochem. J. 383 (Pt 2): 237–48. doi:10.1042/BJ20040647. PMC 1134064. PMID 15242332. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1134064. 
• Adams DJ, Beveridge DJ, van der Weyden L, et al. (2003). "HADHB, HuR, and CP1 bind to the distal 3'-untranslated region of human renin mRNA and differentially modulate renin expression.". J. Biol. Chem. 278 (45): 44894–903. doi:10.1074/jbc.M307782200. PMID 12933794. 
• Spiekerkoetter U, Khuchua Z, Yue Z, et al. (2004). "General mitochondrial trifunctional protein (TFP) deficiency as a result of either alpha- or beta-subunit mutations exhibits similar phenotypes because mutations in either subunit alter TFP complex expression and subunit turnover.". Pediatr. Res. 55 (2): 190–6. doi:10.1203/01.PDR.0000103931.80055.06. PMID 14630990. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• Bogenhagen DF, Rousseau D, Burke S (2008). "The layered structure of human mitochondrial DNA nucleoids.". J. Biol. Chem. 283 (6): 3665–75. doi:10.1074/jbc.M708444200. PMID 18063578. 
• Middleton B (1994). "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase.". Biochem. Soc. Trans. 22 (2): 427–31. PMID 7958339. 
• Zhao Y, Meng XM, Wei YJ, et al. (2003). "Cloning and characterization of a novel cardiac-specific kinase that interacts specifically with cardiac troponin I.". J. Mol. Med. 81 (5): 297–304. doi:10.1007/s00109-003-0427-x. PMID 12721663. 
• Behrends C, Sowa ME, Gygi SP, Harper JW (2010). "Network organization of the human autophagy system.". Nature 466 (7302): 68–76. doi:10.1038/nature09204. PMC 2901998. PMID 20562859. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2901998. 
• Purevsuren J, Fukao T, Hasegawa Y, et al. (2009). "Clinical and molecular aspects of Japanese patients with mitochondrial trifunctional protein deficiency.". Mol. Genet. Metab. 98 (4): 372–7. doi:10.1016/j.ymgme.2009.07.011. PMID 19699128. 
• Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621. 
• Spiekerkoetter U, Sun B, Khuchua Z, et al. (2003). "Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations.". Hum. Mutat. 21 (6): 598–607. doi:10.1002/humu.10211. PMID 12754706. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Fould B, Garlatti V, Neumann E, et al. (2010). "Structural and functional characterization of the recombinant human mitochondrial trifunctional protein.". Biochemistry 49 (39): 8608–17. doi:10.1021/bi100742w. PMID 20825197. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Ibdah JA, Tein I, Dionisi-Vici C, et al. (1998). "Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation.". J. Clin. Invest. 102 (6): 1193–9. doi:10.1172/JCI2091. PMID 9739053. 
• Gevaert K, Goethals M, Martens L, et al. (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
• Hendrickson SL, Lautenberger JA, Chinn LW, et al. (2010). "Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.". PLoS ONE 5 (9): e12862. doi:10.1371/journal.pone.0012862. PMC 2943476. PMID 20877624. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2943476. 
• Frackowiak J, Mazur-Kolecka B, Kaczmarski W, Dickson D (2001). "Deposition of Alzheimer's vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB).". Brain Res. 907 (1-2): 44–53. doi:10.1016/S0006-8993(01)02497-0. PMID 11430884. 

External links

• MeSH HADHB+protein,+human

This article incorporates text from the United States National Library of Medicine, which is in the public domain.