3glk | pdb_00003glk
From Proteopedia
The biotin carboxylase (BC) domain of human Acetyl-CoA Carboxylase 2 (ACC2)
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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 PubMedBODIPY-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 AlsoReferences
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This page was last modified 08:07, 9 March 2022.