OXCT1

3-oxoacid CoA transferase 1
PDB rendering based on 1m3e.
Available structures PDB 1m3e, 1o9l, 1ooy, 1ooz, 1ope
Identifiers
Symbols	OXCT1; OXCT; SCOT
External IDs	OMIM: 601424 MGI: 1914291 HomoloGene: 377 GeneCards: OXCT1 Gene
EC number	2.8.3.5
Gene Ontology Molecular function • 3-oxoacid CoA-transferase activity • 3-oxoacid CoA-transferase activity • transferase activity • protein homodimerization activity Cellular component • mitochondrion • mitochondrion • mitochondrial matrix Biological process • brain development • heart development • response to nutrient • metabolic process • response to hormone stimulus • response to activity • positive regulation of insulin secretion • response to drug • response to starvation • cellular lipid metabolic process • response to ethanol • cellular ketone body metabolic process • cellular ketone body metabolic process • ketone body catabolic process • adipose tissue development • cellular response to acid • cellular response to glucose stimulus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5019	67041
Ensembl	ENSG00000083720	ENSMUSG00000022186
UniProt	P55809	A1E285
RefSeq (mRNA)	NM_000436	NM_024188.6
RefSeq (protein)	NP_000427	NP_077150.1
Location (UCSC)	Chr 5: 41.73 – 41.87 Mb	Chr 15: 3.98 – 4.11 Mb
PubMed search	[1]	[2]

Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial is an enzyme that in humans is encoded by the OXCT1 gene.^[1][2]

This gene encodes a member of the 3-oxoacid CoA-transferase gene family. The encoded protein is a homodimeric mitochondrial matrix enzyme that plays a central role in extrahepatic ketone body catabolism by catalyzing the reversible transfer of coenzyme A from succinyl-CoA to acetoacetate. Mutations in this gene are associated with succinyl CoA:3-oxoacid CoA transferase deficiency.^[2]

See also

• Succinyl-CoA:3-oxoacid CoA transferase deficiency

References

1. ^ Kassovska-Bratinova S, Fukao T, Song XQ, Duncan AM, Chen HS, Robert MF, Perez-Cerda C, Ugarte M, Chartrand C, Vobecky S, Kondo N, Mitchell GA (Sep 1996). "Succinyl CoA: 3-oxoacid CoA transferase (SCOT): human cDNA cloning, human chromosomal mapping to 5p13, and mutation detection in a SCOT-deficient patient". Am J Hum Genet 59 (3): 519–28. PMC 1914926. PMID 8751852. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1914926. 
2. ^ ^{a b} "Entrez Gene: OXCT1 3-oxoacid CoA transferase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5019. 

Further reading

• Pérez-Cerdá C, Merinero B, Sanz P et al. (1992). "A new case of succinyl-CoA: acetoacetate transferase deficiency". J. Inherit. Metab. Dis. 15 (3): 371–3. doi:10.1007/BF02435979. PMID 1405472. 
• Zołnierowicz S, Scisłowski PW, Swierczyński J, Zelewski L (1985). "Acetoacetate utilization by human placental mitochondria". Placenta 5 (3): 271–6. doi:10.1016/S0143-4004(84)80037-5. PMID 6150478. 
• Fukao T, Song XQ, Mitchell GA et al. (1997). "Enzymes of ketone body utilization in human tissues: protein and messenger RNA levels of succinyl-coenzyme A (CoA):3-ketoacid CoA transferase and mitochondrial and cytosolic acetoacetyl-CoA thiolases". Pediatr. Res. 42 (4): 498–502. doi:10.1203/00006450-199710000-00013. PMID 9380443. 
• Song XQ, Fukao T, Watanabe H et al. (1998). "Succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency: two pathogenic mutations, V133E and C456F, in Japanese siblings". Hum. Mutat. 12 (2): 83–8. doi:10.1002/(SICI)1098-1004(1998)12:2<83::AID-HUMU2>3.0.CO;2-P. PMID 9671268. 
• Fukao T, Mitchell GA, Song XQ et al. (2001). "Succinyl-CoA:3-ketoacid CoA transferase (SCOT): cloning of the human SCOT gene, tertiary structural modeling of the human SCOT monomer, and characterization of three pathogenic mutations". Genomics 68 (2): 144–51. doi:10.1006/geno.2000.6282. PMID 10964512. 
• Tanaka H, Kohroki J, Iguchi N et al. (2002). "Cloning and characterization of a human orthologue of testis-specific succinyl CoA: 3-oxo acid CoA transferase (Scot-t) cDNA". Mol. Hum. Reprod. 8 (1): 16–23. doi:10.1093/molehr/8.1.16. PMID 11756565. 
• Strausberg RL, Feingold EA, Grouse LH et al. (2003). "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. 
• 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. 
• 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. 
• Fukao T, Shintaku H, Kusubae R et al. (2005). "Patients homozygous for the T435N mutation of succinyl-CoA:3-ketoacid CoA Transferase (SCOT) do not show permanent ketosis". Pediatr. Res. 56 (6): 858–63. doi:10.1203/01.PDR.0000145297.90577.67. PMID 15496607. 
• Fukao T, Sakurai S, Rolland MO et al. (2006). "A 6-bp deletion at the splice donor site of the first intron resulted in aberrant splicing using a cryptic splice site within exon 1 in a patient with succinyl-CoA: 3-Ketoacid CoA transferase (SCOT) deficiency". Mol. Genet. Metab. 89 (3): 280–2. doi:10.1016/j.ymgme.2006.04.014. PMID 16765626.