COQ2

Identifiers

COQ2, CL640, COQ10D1, MSA1, PHB:PPT, coenzyme Q2, polyprenyltransferase

External IDs

MGI: 1919133 HomoloGene: 69192 GeneCards: COQ2

Gene ontology
Molecular function	• transferase activity • 4-hydroxybenzoate nonaprenyltransferase activity • prenyltransferase activity • 4-hydroxybenzoate decaprenyltransferase activity • transferase activity, transferring alkyl or aryl (other than methyl) groups
Cellular component	• integral component of membrane • mitochondrial inner membrane • membrane • mitochondrion • integral component of mitochondrial inner membrane
Biological process	• glycerol metabolic process • isoprenoid biosynthetic process • ubiquinone biosynthetic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


27235


71883

Ensembl


ENSG00000173085


ENSMUSG00000029319

UniProt


Q96H96


Q66JT7

RefSeq (mRNA)


NM_015697


NM_027978

RefSeq (protein)


NP_056512


NP_082254

Location (UCSC)

Chr 4: 83.26 – 83.28 Mb

Chr 5: 100.65 – 100.68 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Para-hydroxybenzoate—polyprenyltransferase, mitochondrial is an enzyme that in humans is encoded by the COQ2 gene.^[3]^[4]

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]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Forsgren M, Attersand A, Lake S, Grunler J, Swiezewska E, Dallner G, Climent I (Aug 2004). "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. PMC 1133808 . PMID 15153069. doi:10.1042/BJ20040261.
1 2 "Entrez Gene: COQ2 coenzyme Q2 homolog, prenyltransferase (yeast)".

External links

Human COQ2 genome location and COQ2 gene details page in the UCSC Genome Browser.

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. PMC 16267 . PMID 10737800. doi:10.1073/pnas.97.7.3491.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
Esaka Y, Nagahara Y, Hasome Y, et al. (2005). "Coenzyme Q2 induced p53-dependent apoptosis". Biochim. Biophys. Acta. 1724 (1–2): 49–58. PMID 15905035. doi:10.1016/j.bbagen.2005.04.013.
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. PMC 1380241 . PMID 16400613. doi:10.1086/500092.
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. PMID 16643834. doi:10.1016/j.ab.2006.03.029.
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. doi:10.1002/biof.5520250105.
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. PMC 1804361 . PMID 17332895. doi:10.1172/JCI29089.
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. PMID 17374725. doi:10.1093/hmg/ddm058.
Oh J, Ban MR, Miskie BA, et al. (2007). "Genetic determinants of statin intolerance". Lipids in health and disease. 6: 7. PMC 1832194 . PMID 17376224. doi:10.1186/1476-511X-6-7.
Diomedi-Camassei F, Di Giandomenico S, Santorelli FM, et al. (2007). "COQ2 nephropathy: a newly described inherited mitochondriopathy with primary renal involvement". J. Am. Soc. Nephrol. 18 (10): 2773–80. PMID 17855635. doi:10.1681/ASN.2006080833.

Metabolism: Citric acid cycle enzymes

Cycle

Anaplerotic

to acetyl-CoA	Pyruvate dehydrogenase complex (E1, E2, E3) (regulated by Pyruvate dehydrogenase kinase and Pyruvate dehydrogenase phosphatase)
to α-ketoglutaric acid	Glutamate dehydrogenase
to succinyl-CoA	Methylmalonyl-CoA mutase
to oxaloacetate	Pyruvate carboxylase Aspartate transaminase

Mitochondrial
electron transport chain/
oxidative phosphorylation

Primary	Complex I/NADH dehydrogenase Complex II/Succinate dehydrogenase Coenzyme Q Complex III/Coenzyme Q - cytochrome c reductase Cytochrome c Complex IV/Cytochrome c oxidase Coenzyme Q10 synthesis: COQ2 COQ3 COQ4 COQ5 COQ6 COQ7 COQ9 COQ10A COQ10B PDSS1 PDSS2
Other	Alternative oxidase Electron-transferring-flavoprotein dehydrogenase

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COQ2

References

External links

Further reading