Petsko G A, Kenyon G L, Gerlt J A, Ringe D, Kozarich J W
Rosensteil Center, Brandeis University, Waltham, MA 02254.
Trends Biochem Sci. 1993 Oct;18(10):372-6. doi: 10.1016/0968-0004(93)90091-z.
The diversity of enzyme catalytic function is remarkable, particularly when one considers that ancestral life forms must have started with a much smaller ensemble of proteins. In this article, we discuss the evolution of the mandelate pathway in pseudomonads as an example of how catalytic diversity may have evolved. We suggest that existing enzymes that catalyse the chemistry needed to accomplish a transformation were recruited, followed by the evolution of specific binding.
酶催化功能的多样性非常显著,尤其是当人们考虑到原始生命形式最初必定只有数量少得多的蛋白质时。在本文中,我们讨论假单胞菌中扁桃酸途径的进化,以此作为催化多样性可能如何进化的一个例子。我们认为,催化完成一种转化所需化学反应的现有酶被招募进来,随后发生特异性结合的进化。