ACAD8

ACAD8
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1RX0
Identifiers
Aliases	ACAD8, ACAD-8, ARC42, acyl-CoA dehydrogenase family member 8, IBDH
External IDs	OMIM: 604773; MGI: 1914198; HomoloGene: 8662; GeneCards: ACAD8; OMA:ACAD8 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	134,265,855 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	26,910,862 bp
RNA expression pattern
	Top expressed in
	right lobe of thyroid gland; ; left lobe of thyroid gland; ; cerebellar hemisphere; ; body of pancreas; ; right hemisphere of cerebellum; ; apex of heart; ; skin of leg; ; skin of abdomen; ; right frontal lobe; ; right lobe of liver;
	Top expressed in
	right kidney; ; Epithelium of choroid plexus; ; proximal tubule; ; neural layer of retina; ; muscle of thigh; ; granulocyte; ; left lobe of liver; ; human kidney; ; morula; ; spermatocyte;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity, acting on the CH-CH group of donors; oxidoreductase activity; acyl-CoA dehydrogenase activity; flavin adenine dinucleotide binding;
Cellular component	mitochondrial matrix; mitochondrion;
Biological process	valine catabolic process; branched-chain amino acid catabolic process; regulation of transcription, DNA-templated; transcription, DNA-templated; lipid metabolism;
	Sources:Amigo / QuickGO
Orthologs
	27034
	66948
	ENSG00000151498
	ENSMUSG00000031969
	Q9UKU7
	Q9D7B6
	NM_014384
	NM_025862
	NP_055199
	NP_080138
	Wikidata
View/Edit Human	View/Edit Mouse

Isobutyryl-CoA dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ACAD8 gene on chromosome 11.^[5]^[6]

The protein encoded by ACAD8 is a mitochondrial protein belongs to the acyl-CoA dehydrogenase family of enzymes, which function to catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branched-chain amino acids. ACAD8 functions in catabolism of the branched-chain amino acid valine.

Structure

ACAD8 functions as a homotetramer and has an overall structure is similar to other acyl-CoA dehydrogenases. The functional protein contains an NH2-terminal alpha-helical domain, a medial beta-strand domain and a C-terminal alpha-helical domain.^[7]

Clinical significance

Mutations in ACAD8 have been linked to isobutyryl-CoA dehydrogenase deficiency.^[8] Most patients with isobutyryl-CoA dehydrogenase deficiency are asymptotic, but children have also been observed to develop dilated cardiomyopathy.^[9]

Function

ACAD8 is an isobutyryl-CoA dehydrogenase that functions in the catabolism of branched-chain amino acids including valine, and shows high reactivity toward isobutyryl-CoA.^[8] ACAD8 is responsible for the third step in the breakdown of valine and converts isobutyryl-CoA into methylacrylyl-CoA.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000151498 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031969 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Telford EA, Moynihan LM, Markham AF, Lench NJ (Sep 1999). "Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1446 (3): 371–6. doi:10.1016/s0167-4781(99)00102-5. PMID 10524212.
^ "Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8".
^ Battaile KP, Nguyen TV, Vockley J, Kim JJ (2004). "Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases". J. Biol. Chem. 279 (16): 16526–34. doi:10.1074/jbc.M400034200. PMID 14752098.
^ ^a ^b Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J (2002). "Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans" (PDF). Mol. Genet. Metab. 77 (1–2): 68–79. doi:10.1016/S1096-7192(02)00152-X. PMID 12359132.
^ Isobutyryl-CoA dehydrogenase deficiency. Orphanet. 2007; http://www.orpha.net/consor/cgi-bin/OC_Exp.php?Lng=EN&Expert=79159. Accessed 2/8/2010.

External links

Human ACAD8 genome location and ACAD8 gene details page in the UCSC Genome Browser.
Overview of all the structural information available in the PDB for UniProt: Q9UKU7 (Isobutyryl-CoA dehydrogenase, mitochondrial) at the PDBe-KB.

Näär AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R (Apr 1999). "Composite co-activator ARC mediates chromatin-directed transcriptional activation". Nature. 398 (6730): 828–32. Bibcode:1999Natur.398..828N. doi:10.1038/19789. PMID 10235267. S2CID 23646963.
Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F (Nov 2000). "Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism". American Journal of Human Genetics. 67 (5): 1095–103. doi:10.1086/303105. PMC 1288551. PMID 11013134.
Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J (2003). "Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans". Molecular Genetics and Metabolism. 77 (1–2): 68–79. doi:10.1016/S1096-7192(02)00152-X. PMID 12359132.
Battaile KP, Nguyen TV, Vockley J, Kim JJ (Apr 2004). "Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases". The Journal of Biological Chemistry. 279 (16): 16526–34. doi:10.1074/jbc.M400034200. PMID 14752098.
Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC (Mar 2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000151498 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000031969 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10524212-5] Telford EA, Moynihan LM, Markham AF, Lench NJ (Sep 1999). "Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1446 (3): 371–6. doi:10.1016/s0167-4781(99)00102-5. PMID 10524212.

[entrez-6] "Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8".

[7] Battaile KP, Nguyen TV, Vockley J, Kim JJ (2004). "Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases". J. Biol. Chem. 279 (16): 16526–34. doi:10.1074/jbc.M400034200. PMID 14752098.

[ReferenceA-8] Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J (2002). "Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans" (PDF). Mol. Genet. Metab. 77 (1–2): 68–79. doi:10.1016/S1096-7192(02)00152-X. PMID 12359132.

[9] Isobutyryl-CoA dehydrogenase deficiency. Orphanet. 2007; http://www.orpha.net/consor/cgi-bin/OC_Exp.php?Lng=EN&Expert=79159. Accessed 2/8/2010.

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Structure

Clinical significance

Function

References

External links

Further reading