Enzymatic reduction of phenylglyoxal and 2,3-butanedione, two commonly used arginine-modifying reagents, by the ketoacyl reductase domain of fatty acid synthase |
| |
| Authors: | A J Poulose P E Kolattukudy |
| |
| Institution: | 1. Department of Chemical and Biological Engineering, University of Wisconsin-Madison, Madison, WI, USA;2. Department of Chemistry, University of Illinois, Urbana, IL, USA;3. Department of Chemical and Biological Engineering, Iowa State University, Ames, IA, USA;4. Department of Chemical Engineering, The Pennsylvania State University, University Park, PA, USA;5. DOE Center Advanced Bioenergy and Bioproducts Innovation, USA |
| |
| Abstract: | Fatty acid synthase catalyzes the reduction of one of the carbonyl groups in phenylglyoxal and 2,3-butanedione using NADPH as the reductant. Selective inactivation of the enoyl reductase, one of the two reductase domains that could catalyze this reduction, did not affect the carbonyl reduction showing that the ketoreductase domain catalyzed the reaction. The apparent Km for the two arginine-specific reagents were lower than that for 3-acetoacetyl-N-acetyl cysteamine, the commonly used model substrate for the ketoreductase activity of the synthase. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
