Di Cera Enrico
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
J Biol Chem. 2006 Jan 20;281(3):1305-8. doi: 10.1074/jbc.R500023200. Epub 2005 Nov 2.
Enzymes activated by monovalent cations are abundantly represented in plants and the animal world. They have evolved to exploit Na+ and K+, readily available in biological environments, as major driving forces for substrate binding and catalysis. Recent progress in the structural biology of such enzymes has answered long standing questions about the molecular mechanism of activation and the origin of monovalent cation selectivity. That enables a simple classification of these functionally diverse enzymes and reveals unanticipated connections with ion transporters.
由单价阳离子激活的酶在植物和动物界中大量存在。它们已经进化到利用生物环境中容易获得的Na+和K+作为底物结合和催化的主要驱动力。这类酶的结构生物学的最新进展回答了关于激活分子机制和单价阳离子选择性起源的长期问题。这使得对这些功能多样的酶进行简单分类成为可能,并揭示了与离子转运体意想不到的联系。