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'''Isobutyryl-CoA dehydrogenase, mitochondrial''' is an [[enzyme]] that in [[human]]s is encoded by the ''ACAD8'' [[gene]] on chromosome 11.<ref name="pmid10524212">{{cite journal | vauthors = Telford EA, Moynihan LM, Markham AF, Lench NJ | title = Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family | journal = Biochimica et Biophysica Acta | volume = 1446 | issue = 3 | pages = 371–6 | date = Sep 1999 | pmid = 10524212 | pmc =  | doi = 10.1016/s0167-4781(99)00102-5 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27034| accessdate = }}</ref>


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 acid]]s. ACAD8 functions in catabolism of the branched-chain amino acid valine.


'''Acyl-Coenzyme A dehydrogenase family, member 8''', also known as '''ACAD8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27034| accessdate = }}</ref>
== 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.<ref>{{cite journal |vauthors=Battaile KP, Nguyen TV, Vockley J, Kim JJ |title=Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases |journal=J. Biol. Chem. |volume=279 |issue=16 |pages=16526–34 |year=2004 |pmid=14752098 |doi=10.1074/jbc.M400034200 |url=}}</ref>


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== Clinical significance ==
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==References==
Mutations in ACAD8 have been linked to [[isobutyryl-CoA dehydrogenase deficiency]].<ref name="ReferenceA">{{cite journal |vauthors=Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J |title=Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans |journal=Mol. Genet. Metab. |volume=77 |issue=1–2 |pages=68–79 |year=2002 |pmid=12359132 |doi= 10.1016/S1096-7192(02)00152-X|url=}}</ref> Most patients with isobutyryl-CoA dehydrogenase deficiency are asymptotic, but children have also been observed to develop [[dilated cardiomyopathy]].<ref>Isobutyryl-CoA dehydrogenase deficiency. Orphanet. 2007; http://www.orpha.net/consor/cgi-bin/OC_Exp.php?Lng=EN&Expert=79159. Accessed 2/8/2010.</ref>
 
== Function ==
 
ACAD8 is an isobutyryl-CoA [[dehydrogenase]] that functions in the catabolism of [[branched-chain amino acid]]s including [[valine]], and shows high reactivity toward isobutyryl-CoA.<ref name="ReferenceA"/> ACAD8 is responsible for the third step in the breakdown of valine and converts isobutyryl-CoA into methylacrylyl-CoA.
 
== References ==
{{reflist}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ACAD8}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Näär AM, Beaurang PA, Zhou S, Abraham S, Solomon W, Tjian R | title = Composite co-activator ARC mediates chromatin-directed transcriptional activation | journal = Nature | volume = 398 | issue = 6730 | pages = 828–32 | date = Apr 1999 | pmid = 10235267 | doi = 10.1038/19789 }}
| citations =
* {{cite journal | vauthors = 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 | title = 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 | journal = American Journal of Human Genetics | volume = 67 | issue = 5 | pages = 1095–103 | date = Nov 2000 | pmid = 11013134 | pmc = 1288551 | doi = 10.1086/303105 }}
*{{cite journal | author=Näär AM, Beaurang PA, Zhou S, ''et al.'' |title=Composite co-activator ARC mediates chromatin-directed transcriptional activation. |journal=Nature |volume=398 |issue= 6730 |pages= 828–32 |year= 1999 |pmid= 10235267 |doi= 10.1038/19789 }}
* {{cite journal | vauthors = Nguyen TV, Andresen BS, Corydon TJ, Ghisla S, Abd-El Razik N, Mohsen AW, Cederbaum SD, Roe DS, Roe CR, Lench NJ, Vockley J | title = Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans | journal = Molecular Genetics and Metabolism | volume = 77 | issue = 1–2 | pages = 68–79 | year = 2003 | pmid = 12359132 | doi = 10.1016/S1096-7192(02)00152-X }}
*{{cite journal | author=Telford EA, Moynihan LM, Markham AF, Lench NJ |title=Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 3 |pages= 371–6 |year= 1999 |pmid= 10524212 |doi=  }}
* {{cite journal | vauthors = Battaile KP, Nguyen TV, Vockley J, Kim JJ | title = Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases | journal = The Journal of Biological Chemistry | volume = 279 | issue = 16 | pages = 16526–34 | date = Apr 2004 | pmid = 14752098 | doi = 10.1074/jbc.M400034200 }}
*{{cite journal  | author=Andresen BS, Christensen E, Corydon TJ, ''et al.'' |title=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. |journal=Am. J. Hum. Genet. |volume=67 |issue= 5 |pages= 1095–103 |year= 2000 |pmid= 11013134 |doi= }}
* {{cite journal | vauthors = Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC | title = Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects | journal = Atherosclerosis | volume = 191 | issue = 1 | pages = 63–72 | date = Mar 2007 | pmid = 16806233 | doi = 10.1016/j.atherosclerosis.2006.05.032 }}
*{{cite journal | author=Nguyen TV, Andresen BS, Corydon TJ, ''et al.'' |title=Identification of isobutyryl-CoA dehydrogenase and its deficiency in humans. |journal=Mol. Genet. Metab. |volume=77 |issue= 1-2 |pages= 68–79 |year= 2003 |pmid= 12359132 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Battaile KP, Nguyen TV, Vockley J, Kim JJ |title=Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases. |journal=J. Biol. Chem. |volume=279 |issue= 16 |pages= 16526–34 |year= 2004 |pmid= 14752098 |doi= 10.1074/jbc.M400034200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Ma J, Dempsey AA, Stamatiou D, ''et al.'' |title=Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects. |journal=Atherosclerosis |volume=191 |issue= 1 |pages= 63–72 |year= 2007 |pmid= 16806233 |doi= 10.1016/j.atherosclerosis.2006.05.032 }}
}}
{{refend}}
{{refend}}


{{PDB Gallery|geneid=27034}}


[[Category:Human proteins]]


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Latest revision as of 17:42, 29 August 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Isobutyryl-CoA dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ACAD8 gene on chromosome 11.[1][2]

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.[3]

Clinical significance

Mutations in ACAD8 have been linked to isobutyryl-CoA dehydrogenase deficiency.[4] Most patients with isobutyryl-CoA dehydrogenase deficiency are asymptotic, but children have also been observed to develop dilated cardiomyopathy.[5]

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.[4] ACAD8 is responsible for the third step in the breakdown of valine and converts isobutyryl-CoA into methylacrylyl-CoA.

References

  1. ↑ 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. 1446 (3): 371–6. doi:10.1016/s0167-4781(99)00102-5. PMID 10524212.
  2. ↑ "Entrez Gene: ACAD8 acyl-Coenzyme A dehydrogenase family, member 8".
  3. ↑ 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.
  4. ↑ 4.0 4.1 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". Mol. Genet. Metab. 77 (1–2): 68–79. doi:10.1016/S1096-7192(02)00152-X. PMID 12359132.
  5. ↑ 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

Further reading


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