Structural highlights
Function
[ACACB_HUMAN] ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
BODIPY-labeled Soraphen A derivative 4 was synthesized and characterized as an acetyl-CoA carboxylase (ACC) binder. Biophysical measurements indicate that the molecule binds in the biotin carboxylase domain where Soraphen A has been shown to bind. The fluorescent label of the BODIPY can be used to biophysically identify a compound that binds to the Soraphen A site of the biotin carboxylase domain versus the carboxytransferase domain of ACC.
Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase.,Raymer B, Kavana M, Price A, Wang B, Corcoran L, Kulathila R, Groarke J, Mann T Bioorg Med Chem Lett. 2009 May 15;19(10):2804-7. doi: 10.1016/j.bmcl.2009.03.107., Epub 2009 Mar 26. PMID:19359168[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Raymer B, Kavana M, Price A, Wang B, Corcoran L, Kulathila R, Groarke J, Mann T. Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase. Bioorg Med Chem Lett. 2009 May 15;19(10):2804-7. doi: 10.1016/j.bmcl.2009.03.107., Epub 2009 Mar 26. PMID:19359168 doi:http://dx.doi.org/10.1016/j.bmcl.2009.03.107
