Biology:ACACA
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Acetyl-CoA carboxylase 1 also known as ACC-alpha or ACCa is an enzyme that in humans is encoded by the ACACA gene.[1][2]
Function
Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA.[1]
References
- ↑ 1.0 1.1 "Entrez Gene: acetyl-Coenzyme A carboxylase alpha". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=31.
- ↑ "Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms". Proceedings of the National Academy of Sciences of the United States of America 92 (9): 4011–5. April 1995. doi:10.1073/pnas.92.9.4011. PMID 7732023. Bibcode: 1995PNAS...92.4011A.
Further reading
- "Haplotype-based analysis of common variation in the acetyl-coA carboxylase alpha gene and breast cancer risk: a case-control study nested within the European Prospective Investigation into Cancer and Nutrition". Cancer Epidemiology, Biomarkers & Prevention 16 (3): 409–15. March 2007. doi:10.1158/1055-9965.EPI-06-0617. PMID 17372234.
- "Acetyl-coenzyme A carboxylase alpha gene variations may be associated with the direct effects of some antipsychotics on triglyceride levels". Schizophrenia Research 115 (2–3): 136–40. December 2009. doi:10.1016/j.schres.2009.09.038. PMID 19846279.
- "Myocardial hypertrophy and the maturation of fatty acid oxidation in the newborn human heart". Pediatric Research 64 (6): 643–7. December 2008. doi:10.1203/PDR.0b013e318184d281. PMID 18614968.
- "Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins". Proteomics 9 (9): 2444–56. May 2009. doi:10.1002/pmic.200800738. PMID 19343720.
- "Up-regulation of acetyl-CoA carboxylase alpha and fatty acid synthase by human epidermal growth factor receptor 2 at the translational level in breast cancer cells". The Journal of Biological Chemistry 282 (36): 26122–31. September 2007. doi:10.1074/jbc.M702854200. PMID 17631500.
- "Exploring genetic variations that may be associated with the direct effects of some antipsychotics on lipid levels". Schizophrenia Research 98 (1–3): 40–6. January 2008. doi:10.1016/j.schres.2007.10.003. PMID 18031993.
- "Kidney bean husk extracts exert antitumor effect by inducing apoptosis involving AMP-activated protein kinase signaling pathway". Annals of the New York Academy of Sciences 1171 (1): 484–8. August 2009. doi:10.1111/j.1749-6632.2009.04697.x. PMID 19723093. Bibcode: 2009NYASA1171..484L.
- "Acute exercise does not cause sustained elevations in AMPK signaling or expression". Medicine and Science in Sports and Exercise 40 (8): 1490–4. August 2008. doi:10.1249/MSS.0b013e318173a037. PMID 18614941.
- "Multiple genetic variants along candidate pathways influence plasma high-density lipoprotein cholesterol concentrations". Journal of Lipid Research 49 (12): 2582–9. December 2008. doi:10.1194/jlr.M800232-JLR200. PMID 18660489.
- "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. May 2006. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
- Bonini, Marcelo, ed (2009). "Inhibition of stearoylCoA desaturase-1 inactivates acetyl-CoA carboxylase and impairs proliferation in cancer cells: role of AMPK". PLOS ONE 4 (8): e6812. doi:10.1371/journal.pone.0006812. PMID 19710915. Bibcode: 2009PLoSO...4.6812S.
- "Fine expression profiling of full-length transcripts using a size-unbiased cDNA library prepared with the vector-capping method". DNA Research 15 (3): 123–36. June 2008. doi:10.1093/dnares/dsn010. PMID 18487259.
- "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. November 2006. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- "Specific pattern of LKB1 and phospho-acetyl-CoA carboxylase protein immunostaining in human normal tissues and lung carcinomas". Human Pathology 38 (9): 1351–60. September 2007. doi:10.1016/j.humpath.2007.01.022. PMID 17521700.
- "Cell cycle regulation of the BRCA1/acetyl-CoA-carboxylase complex". Biochemical and Biophysical Research Communications 378 (3): 615–9. January 2009. doi:10.1016/j.bbrc.2008.11.090. PMID 19061860.
- "Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells". The Journal of Biological Chemistry 283 (6): 3418–23. February 2008. doi:10.1074/jbc.M707650200. PMID 18056116.
- "Differential activation of recombinant human acetyl-CoA carboxylases 1 and 2 by citrate". Archives of Biochemistry and Biophysics 475 (1): 72–9. July 2008. doi:10.1016/j.abb.2008.04.011. PMID 18455495.
- "Physiogenomic comparison of edema and BMI in patients receiving rosiglitazone or pioglitazone". Clinica Chimica Acta; International Journal of Clinical Chemistry 400 (1–2): 48–55. February 2009. doi:10.1016/j.cca.2008.10.009. PMID 18996102.
- "Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1". Biochemistry 47 (21): 5767–73. May 2008. doi:10.1021/bi800314m. PMID 18452305.
External links
- Human ACACA genome location and ACACA gene details page in the UCSC Genome Browser.
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