COQ2

From Wikipedia, the free encyclopedia

Coenzyme Q2 homolog, prenyltransferase (yeast)

Identifiers

COQ2; CL640; FLJ26072

External IDs

OMIM: 609825 MGI: 1919133 HomoloGene: 69192

Gene ontology
Molecular Function:	• prenyltransferase activity • transferase activity
Cellular Component:	• mitochondrion • membrane • integral to membrane
Biological Process:	• glycerol metabolic process • ubiquinone biosynthetic process • isoprenoid biosynthetic process • biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_015697 (mRNA)
NP_056512 (protein)

NM_027978 (mRNA)
NP_082254 (protein)

Location

Chr 4: 84.4 - 84.43 Mb

n/a

Pubmed search

[1]

[2]

Coenzyme Q2 homolog, prenyltransferase (yeast), also known as COQ2, is a human gene.^[1]

CoQ (ubiquinone) serves as a redox carrier in the mitochondrial respiratory chain and is a lipid-soluble antioxidant. COQ2, or parahydroxybenzoate-polyprenyltransferase (EC 2.5.1.39), catalyzes one of the final reactions in the biosynthesis of CoQ, the prenylation of parahydroxybenzoate with an all-trans polyprenyl group (Forsgren et al., 2004).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: COQ2 coenzyme Q2 homolog, prenyltransferase (yeast).

[edit] Further reading

Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags.". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491-6. PMID 10737800.
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. PMID 12477932.
Forsgren M, Attersand A, Lake S, et al. (2005). "Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ.". Biochem. J. 382 (Pt 2): 519-26. doi:10.1042/BJ20040261. PMID 15153069.
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. PMID 15489334.
Esaka Y, Nagahara Y, Hasome Y, et al. (2005). "Coenzyme Q2 induced p53-dependent apoptosis.". Biochim. Biophys. Acta 1724 (1-2): 49-58. doi:10.1016/j.bbagen.2005.04.013. PMID 15905035.
Quinzii C, Naini A, Salviati L, et al. (2007). "A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency.". Am. J. Hum. Genet. 78 (2): 345-9. doi:10.1086/500092. PMID 16400613.
Burón MI, Hermán MD, Alcaín FJ, Villalba JM (2006). "Stimulation of polyprenyl 4-hydroxybenzoate transferase activity by sodium cholate and 3-[(cholamidopropyl)dimethylammonio]-1-propanesulfonate.". Anal. Biochem. 353 (1): 15-21. doi:10.1016/j.ab.2006.03.029. PMID 16643834.
González-Aragón D, Burón MI, López-Lluch G, et al. (2006). "Coenzyme Q and the regulation of intracellular steady-state levels of superoxide in HL-60 cells.". Biofactors 25 (1-4): 31-41. PMID 16873928.
Mollet J, Giurgea I, Schlemmer D, et al. (2007). "Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders.". J. Clin. Invest. 117 (3): 765-72. doi:10.1172/JCI29089. PMID 17332895.
López-Martín JM, Salviati L, Trevisson E, et al. (2007). "Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis.". Hum. Mol. Genet. 16 (9): 1091-7. doi:10.1093/hmg/ddm058. PMID 17374725.
Oh J, Ban MR, Miskie BA, et al. (2007). "Genetic determinants of statin intolerance.". Lipids in health and disease 6: 7. doi:10.1186/1476-511X-6-7. PMID 17376224.
Diomedi-Camassei F, Di Giandomenico S, Santorelli FM, et al.. "COQ2 nephropathy: a newly described inherited mitochondriopathy with primary renal involvement.". J. Am. Soc. Nephrol. 18 (10): 2773-80. doi:10.1681/ASN.2006080833. PMID 17855635.