Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes
Acetyl coenzyme A (acetyl-CoA) carboxylase isozyme 1 (ACC1) and acetyl-CoA carboxylase isozyme 2 (ACC2) are critical for de novo fatty acid synthesis and for the regulation of beta-oxidation. Emerging evidence indicates that one or both isozymes might be therapeutic targets for the treatment of obes...
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| Veröffentlicht in: | Protein expression and purification 2007-01, Vol.51 (1), p.11-21 |
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| container_title | Protein expression and purification |
| container_volume | 51 |
| creator | Cheng, Dong Chu, Ching-Hsuen Chen, Luping Feder, John N Mintier, Gabe A Wu, Yuli Cook, Joseph W Harpel, Mark R Locke, Gregory A An, Yongmi Tamura, James K |
| description | Acetyl coenzyme A (acetyl-CoA) carboxylase isozyme 1 (ACC1) and acetyl-CoA carboxylase isozyme 2 (ACC2) are critical for de novo fatty acid synthesis and for the regulation of beta-oxidation. Emerging evidence indicates that one or both isozymes might be therapeutic targets for the treatment of obesity, type 2 diabetes, and dyslipidemia. One of the major obstacles in the field is the lack of readily-available source of recombinant human ACC enzymes to support systematic drug discovery efforts. Here, we describe an efficient and optimal protocol for expressing and isolating recombinant mammalian ACCs with high yield and purity. The resultant human ACC2, human ACC1, and rat ACC2 possess high specific activities, are properly biotinylated, and exhibit kinetic parameters very similar to the native ACC enzymes. We believe that the current study paves a road to a systematic approach for drug design revolving around the ACC inhibition mechanism. |
| doi_str_mv | 10.1016/j.pep.2006.06.005 |
| format | Article |
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Emerging evidence indicates that one or both isozymes might be therapeutic targets for the treatment of obesity, type 2 diabetes, and dyslipidemia. One of the major obstacles in the field is the lack of readily-available source of recombinant human ACC enzymes to support systematic drug discovery efforts. Here, we describe an efficient and optimal protocol for expressing and isolating recombinant mammalian ACCs with high yield and purity. The resultant human ACC2, human ACC1, and rat ACC2 possess high specific activities, are properly biotinylated, and exhibit kinetic parameters very similar to the native ACC enzymes. 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| ispartof | Protein expression and purification, 2007-01, Vol.51 (1), p.11-21 |
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| subjects | Acetyl-CoA Carboxylase - antagonists & inhibitors Acetyl-CoA Carboxylase - biosynthesis Acetyl-CoA Carboxylase - isolation & purification Acetyl-CoA Carboxylase - metabolism Animals Baculoviridae Chromatography, Affinity Citric Acid - pharmacology Cloning, Molecular - methods Humans Isoenzymes - antagonists & inhibitors Isoenzymes - biosynthesis Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Malonyl Coenzyme A - pharmacology Rats Recombinant Proteins - isolation & purification Streptavidin - chemistry |
| title | Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes |
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