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{{PBB|geneid=32}}
#REDIRECT [[Acetyl-CoA carboxylase]]
'''Acetyl-CoA carboxylase 2''' also known as '''ACC-beta''' or '''ACC2''' is an [[enzyme]] that in humans is encoded by the ''ACACB'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: acetyl-Coenzyme A carboxylase beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=32| accessdate = }}</ref><ref name="pmid8670171">{{cite journal | author = Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA | title = Identification of a second human acetyl-CoA carboxylase gene | journal = Biochem. J. | volume = 316 ( Pt 3) | issue = | pages = 915–22 | year = 1996 | month = June | pmid = 8670171 | pmc = 1217437 | doi = | url = | issn = }}</ref>

== 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. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit [[carnitine palmitoyltransferase I]], the rate-limiting step in fatty acid uptake and oxidation by [[mitochondria]]. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis.<ref name="entrez"/>

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
*{{cite journal |author=Cheng D, Chu CH, Chen L, ''et al.'' |title=Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes. |journal=Protein Expr. Purif. |volume=51 |issue= 1 |pages= 11-21 |year= 2007 |pmid= 16854592 |doi= 10.1016/j.pep.2006.06.005 }}
*{{cite journal |author=Diaz FJ, Meary A, Arranz MJ, ''et al.'' |title=Acetyl-coenzyme A carboxylase alpha gene variations may be associated with the direct effects of some antipsychotics on triglyceride levels. |journal=Schizophr. Res. |volume=115 |issue= 2-3 |pages= 136-40 |year= 2009 |pmid= 19846279 |doi= 10.1016/j.schres.2009.09.038 }}
*{{cite journal |author=Madauss KP, Burkhart WA, Consler TG, ''et al.'' |title=The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twist. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=65 |issue= Pt 5 |pages= 449-61 |year= 2009 |pmid= 19390150 |doi= 10.1107/S0907444909008014 }}
*{{cite journal |author=Kahn BB, Alquier T, Carling D, Hardie DG |title=AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. |journal=Cell Metab. |volume=1 |issue= 1 |pages= 15-25 |year= 2005 |pmid= 16054041 |doi= 10.1016/j.cmet.2004.12.003 }}
*{{cite journal |author=de Leon J, Correa JC, Ruaño G, ''et al.'' |title=Exploring genetic variations that may be associated with the direct effects of some antipsychotics on lipid levels. |journal=Schizophr. Res. |volume=98 |issue= 1-3 |pages= 40-6 |year= 2008 |pmid= 18031993 |doi= 10.1016/j.schres.2007.10.003 }}
*{{cite journal |author=Kreuz S, Schoelch C, Thomas L, ''et al.'' |title=Acetyl-CoA carboxylases 1 and 2 show distinct expression patterns in rats and humans and alterations in obesity and diabetes. |journal=Diabetes Metab. Res. Rev. |volume=25 |issue= 6 |pages= 577-86 |year= 2009 |pmid= 19618481 |doi= 10.1002/dmrr.997 }}
*{{cite journal |author=Castle JC, Hara Y, Raymond CK, ''et al.'' |title=ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected]. |journal=PLoS ONE |volume=4 |issue= 2 |pages= e4369 |year= 2009 |pmid= 19190759 |doi= 10.1371/journal.pone.0004369 }}
*{{cite journal |author=Højlund K, Mustard KJ, Staehr P, ''et al.'' |title=AMPK activity and isoform protein expression are similar in muscle of obese subjects with and without type 2 diabetes. |journal=Am. J. Physiol. Endocrinol. Metab. |volume=286 |issue= 2 |pages= E239-44 |year= 2004 |pmid= 14532170 |doi= 10.1152/ajpendo.00326.2003 }}
*{{cite journal |author=Barbe L, Lundberg E, Oksvold P, ''et al.'' |title=Toward a confocal subcellular atlas of the human proteome. |journal=Mol. Cell Proteomics |volume=7 |issue= 3 |pages= 499-508 |year= 2008 |pmid= 18029348 |doi= 10.1074/mcp.M700325-MCP200 }}
*{{cite journal |author=Szabo de Edelenyi F, Goumidi L, Bertrais S, ''et al.'' |title=Prediction of the metabolic syndrome status based on dietary and genetic parameters, using Random Forest. |journal=Genes & nutrition |volume=3 |issue= 3-4 |pages= 173-6 |year= 2008 |pmid= 19034549 |doi= 10.1007/s12263-008-0097-y }}
*{{cite journal |author=Conde E, Suarez-Gauthier A, García-García E, ''et al.'' |title=Specific pattern of LKB1 and phospho-acetyl-CoA carboxylase protein immunostaining in human normal tissues and lung carcinomas. |journal=Hum. Pathol. |volume=38 |issue= 9 |pages= 1351-60 |year= 2007 |pmid= 17521700 |doi= 10.1016/j.humpath.2007.01.022 }}
*{{cite journal |author=Rosa G, Manco M, Vega N, ''et al.'' |title=Decreased muscle acetyl-coenzyme A carboxylase 2 mRNA and insulin resistance in formerly obese subjects. |journal=Obes. Res. |volume=11 |issue= 11 |pages= 1306-12 |year= 2003 |pmid= 14627750 |doi= 10.1038/oby.2003.177 }}
*{{cite journal |author=Oh SY, Lee MY, Kim JM, ''et al.'' |title=Alternative usages of multiple promoters of the acetyl-CoA carboxylase beta gene are related to differential transcriptional regulation in human and rodent tissues. |journal=J. Biol. Chem. |volume=280 |issue= 7 |pages= 5909-16 |year= 2005 |pmid= 15590647 |doi= 10.1074/jbc.M409037200 }}
*{{cite journal |author=Locke GA, Cheng D, Witmer MR, ''et al.'' |title=Differential activation of recombinant human acetyl-CoA carboxylases 1 and 2 by citrate. |journal=Arch. Biochem. Biophys. |volume=475 |issue= 1 |pages= 72-9 |year= 2008 |pmid= 18455495 |doi= 10.1016/j.abb.2008.04.011 }}
*{{cite journal |author=Cho YS, Lee JI, Shin D, ''et al.'' |title=Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK. |journal=Biochem. Biophys. Res. Commun. |volume=391 |issue= 1 |pages= 187-92 |year= 2010 |pmid= 19900410 |doi= 10.1016/j.bbrc.2009.11.029 }}
*{{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= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal |author=Frøsig C, Jørgensen SB, Hardie DG, ''et al.'' |title=5'-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle. |journal=Am. J. Physiol. Endocrinol. Metab. |volume=286 |issue= 3 |pages= E411-7 |year= 2004 |pmid= 14613924 |doi= 10.1152/ajpendo.00317.2003 }}
*{{cite journal |author=Ruaño G, Bernene J, Windemuth A, ''et al.'' |title=Physiogenomic comparison of edema and BMI in patients receiving rosiglitazone or pioglitazone. |journal=Clin. Chim. Acta |volume=400 |issue= 1-2 |pages= 48-55 |year= 2009 |pmid= 18996102 |doi= 10.1016/j.cca.2008.10.009 }}
*{{cite journal |author=Kim KW, Yamane H, Zondlo J, ''et al.'' |title=Expression, purification, and characterization of human acetyl-CoA carboxylase 2. |journal=Protein Expr. Purif. |volume=53 |issue= 1 |pages= 16-23 |year= 2007 |pmid= 17223360 |doi= 10.1016/j.pep.2006.11.021 }}
*{{cite journal |author=Ruderman N, Prentki M |title=AMP kinase and malonyl-CoA: targets for therapy of the metabolic syndrome. |journal=Nat Rev Drug Discov |volume=3 |issue= 4 |pages= 340-51 |year= 2004 |pmid= 15060529 |doi= 10.1038/nrd1344 }}
{{refend}}

{{gene-12-stub}}

[[Category:EC 6.4.1]]

Revision as of 16:38, 8 April 2010

Template:PBB Acetyl-CoA carboxylase 2 also known as ACC-beta or ACC2 is an enzyme that in humans is encoded by the ACACB 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. ACC-beta is thought to control fatty acid oxidation by means of the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I, the rate-limiting step in fatty acid uptake and oxidation by mitochondria. ACC-beta may be involved in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis.[1]

References

  1. ^ a b "Entrez Gene: acetyl-Coenzyme A carboxylase beta".
  2. ^ Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA (1996). "Identification of a second human acetyl-CoA carboxylase gene". Biochem. J. 316 ( Pt 3): 915–22. PMC 1217437. PMID 8670171. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

Further reading

  • Cheng D, Chu CH, Chen L; et al. (2007). "Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes". Protein Expr. Purif. 51 (1): 11–21. doi:10.1016/j.pep.2006.06.005. PMID 16854592. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Diaz FJ, Meary A, Arranz MJ; et al. (2009). "Acetyl-coenzyme A carboxylase alpha gene variations may be associated with the direct effects of some antipsychotics on triglyceride levels". Schizophr. Res. 115 (2–3): 136–40. doi:10.1016/j.schres.2009.09.038. PMID 19846279. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Madauss KP, Burkhart WA, Consler TG; et al. (2009). "The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twist". Acta Crystallogr. D Biol. Crystallogr. 65 (Pt 5): 449–61. doi:10.1107/S0907444909008014. PMID 19390150. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Kahn BB, Alquier T, Carling D, Hardie DG (2005). "AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism". Cell Metab. 1 (1): 15–25. doi:10.1016/j.cmet.2004.12.003. PMID 16054041.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • de Leon J, Correa JC, Ruaño G; et al. (2008). "Exploring genetic variations that may be associated with the direct effects of some antipsychotics on lipid levels". Schizophr. Res. 98 (1–3): 40–6. doi:10.1016/j.schres.2007.10.003. PMID 18031993. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Kreuz S, Schoelch C, Thomas L; et al. (2009). "Acetyl-CoA carboxylases 1 and 2 show distinct expression patterns in rats and humans and alterations in obesity and diabetes". Diabetes Metab. Res. Rev. 25 (6): 577–86. doi:10.1002/dmrr.997. PMID 19618481. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Castle JC, Hara Y, Raymond CK; et al. (2009). "ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus [corrected]". PLoS ONE. 4 (2): e4369. doi:10.1371/journal.pone.0004369. PMID 19190759. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  • Højlund K, Mustard KJ, Staehr P; et al. (2004). "AMPK activity and isoform protein expression are similar in muscle of obese subjects with and without type 2 diabetes". Am. J. Physiol. Endocrinol. Metab. 286 (2): E239-44. doi:10.1152/ajpendo.00326.2003. PMID 14532170. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Barbe L, Lundberg E, Oksvold P; et al. (2008). "Toward a confocal subcellular atlas of the human proteome". Mol. Cell Proteomics. 7 (3): 499–508. doi:10.1074/mcp.M700325-MCP200. PMID 18029348. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  • Szabo de Edelenyi F, Goumidi L, Bertrais S; et al. (2008). "Prediction of the metabolic syndrome status based on dietary and genetic parameters, using Random Forest". Genes & nutrition. 3 (3–4): 173–6. doi:10.1007/s12263-008-0097-y. PMID 19034549. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Conde E, Suarez-Gauthier A, García-García E; et al. (2007). "Specific pattern of LKB1 and phospho-acetyl-CoA carboxylase protein immunostaining in human normal tissues and lung carcinomas". Hum. Pathol. 38 (9): 1351–60. doi:10.1016/j.humpath.2007.01.022. PMID 17521700. {{cite journal}}: Explicit use of et al. in: |author= (help); soft hyphen character in |author= at position 34 (help)CS1 maint: multiple names: authors list (link)
  • Rosa G, Manco M, Vega N; et al. (2003). "Decreased muscle acetyl-coenzyme A carboxylase 2 mRNA and insulin resistance in formerly obese subjects". Obes. Res. 11 (11): 1306–12. doi:10.1038/oby.2003.177. PMID 14627750. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Oh SY, Lee MY, Kim JM; et al. (2005). "Alternative usages of multiple promoters of the acetyl-CoA carboxylase beta gene are related to differential transcriptional regulation in human and rodent tissues". J. Biol. Chem. 280 (7): 5909–16. doi:10.1074/jbc.M409037200. PMID 15590647. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  • Locke GA, Cheng D, Witmer MR; et al. (2008). "Differential activation of recombinant human acetyl-CoA carboxylases 1 and 2 by citrate". Arch. Biochem. Biophys. 475 (1): 72–9. doi:10.1016/j.abb.2008.04.011. PMID 18455495. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Cho YS, Lee JI, Shin D; et al. (2010). "Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK". Biochem. Biophys. Res. Commun. 391 (1): 187–92. doi:10.1016/j.bbrc.2009.11.029. PMID 19900410. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2002). "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. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Frøsig C, Jørgensen SB, Hardie DG; et al. (2004). "5'-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle". Am. J. Physiol. Endocrinol. Metab. 286 (3): E411-7. doi:10.1152/ajpendo.00317.2003. PMID 14613924. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Ruaño G, Bernene J, Windemuth A; et al. (2009). "Physiogenomic comparison of edema and BMI in patients receiving rosiglitazone or pioglitazone". Clin. Chim. Acta. 400 (1–2): 48–55. doi:10.1016/j.cca.2008.10.009. PMID 18996102. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Kim KW, Yamane H, Zondlo J; et al. (2007). "Expression, purification, and characterization of human acetyl-CoA carboxylase 2". Protein Expr. Purif. 53 (1): 16–23. doi:10.1016/j.pep.2006.11.021. PMID 17223360. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  • Ruderman N, Prentki M (2004). "AMP kinase and malonyl-CoA: targets for therapy of the metabolic syndrome". Nat Rev Drug Discov. 3 (4): 340–51. doi:10.1038/nrd1344. PMID 15060529.
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