Coleman J E
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510.
Annu Rev Biochem. 1992;61:897-946. doi: 10.1146/annurev.bi.61.070192.004341.
In the past five years there has been a great expansion in our knowledge of the role of zinc in the structure and function of proteins. Not only is zinc required for essential catalytic functions in enzymes (more than 300 are known at present), but also it stabilizes and even induces the folding of protein subdomains. The latter functions have been most dramatically illustrated by the discovery of the essential role of zinc in the folding of the DNA-binding domains of eukaryotic transcription factors, including the zinc finger transcription factors, the large family of hormone receptor proteins, and the zinc cluster transcription factors from yeasts. Similar functions are highly probable for the zinc found in the RNA polymerases and the zinc-containing accessory proteins involved in nucleic acid replication. The rapid increase in the number and nature of the proteins in which zinc functions is not unexpected since zinc is the second most abundant trace metal found in eukaryotic organisms, second only to iron. If one subtracts the amount of iron found in hemoglobin, zinc becomes the most abundant trace metal found in the human body.
在过去五年里，我们对锌在蛋白质结构和功能中所起作用的认识有了极大的扩展。锌不仅是酶发挥基本催化功能所必需的（目前已知有300多种酶），而且它能稳定甚至诱导蛋白质亚结构域的折叠。锌在真核转录因子（包括锌指转录因子、一大类激素受体蛋白以及酵母中的锌簇转录因子）的DNA结合结构域折叠中发挥的关键作用的发现，最为生动地说明了后者的功能。在RNA聚合酶以及参与核酸复制的含锌辅助蛋白中发现的锌，很可能也具有类似功能。锌发挥作用的蛋白质数量和种类迅速增加并不意外，因为锌是真核生物中含量第二丰富的痕量金属，仅次于铁。如果减去血红蛋白中的铁含量，锌就成为人体中含量最丰富的痕量金属。
