Covalent modification of lysine residues in various proteins in the nucleus is a recognized mechanism for control of transcription. Now, two papers suggest that acetylation may represent an important regulatory mechanism controlling the function of metabolic enzymes (see the Perspective by Norvell and McMahon). Zhao et al. found that a large proportion of enzymes in various metabolic pathways were acetylated in human liver cells. Acetylation regulated various enzymes by distinct mechanisms, directly activating some, inhibiting one, and controlling the stability of another. Control of metabolism by acetylation appears to be evolutionarily conserved: Wang et al. found that the ability of the bacterium Salmonella enterica to optimize growth on distinct carbon sources required differential acetylation of key metabolic enzymes, thus controlling flux through metabolic pathways.
Q. Wang, Y. Zhang, C. Yang, H. Xiong, Y. Lin, J. Yao, H. Li, L. Xie, W. Zhao, Y. Yao, Z.-B. Ning, R. Zeng, Y. Xiong, K.-L. Guan, S. Zhao, G.-P. Zhao, Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327, 1004–1007 (2010). [Abstract] [Full Text]
S. Zhao, W. Xu, W. Jiang, W. Yu, Y. Lin, T. Zhang, J. Yao, L. Zhou, Y. Zeng, H. Li, Y. Li, J. Shi, W. An, S. M. Hancock, F. He, L. Qin, J. Chin, P. Yang, X. Chen, Q. Lei, Y. Xiong, K.-L. Guan, Regulation of cellular metabolism by protein lysine acetylation. Science 327, 1000–1004 (2010). [Abstract] [Full Text]