酵母甲硫氨酸氨肽酶I可将Zn2+或Co2+用作辅因子：身份误认的案例？
Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: a case of mistaken identity?
作者信息
Walker K W, Bradshaw R A
机构信息
Department of Physiology and Biophysics, College of Medicine, University of California, Irvine 92697, USA.
出版信息
Protein Sci. 1998 Dec;7(12):2684-7. doi: 10.1002/pro.5560071224.
Abstract
Yeast methionine aminopeptidase I (MetAP I) is one of two enzymes in Saccharomyces cerevisiae that is responsible for cotranslational cleavage of initiator methionines. It has previously been classified as a Co2+ metalloprotease in all prokaryotic and eukaryotic forms studied. However, treatment of recombinant apo-MetAP I with 12.5 microM Zn2+ produces an enzyme that is as active as that reconstituted with 200 microM Co2+. In the presence of physiological concentrations of reduced glutathione (GSH), Co-MetAP I is inactive, while the activity of Zn-MetAP I is increased more than 1.7-fold over Zn-MetAP I assayed in the absence of GSH. Given that the in vivo concentration of Zn2+ is at least 1,000-fold higher than that of Co2+, and that Co2+ is insoluble in physiological concentrations of GSH, it is probable that yeast MetAP I is actually a Zn2+ metalloprotease. Furthermore, unless there are extraordinary conditions that insulate or sequester them from this reducing milieu, that have yet to be identified, there are not likely to be any cytoplasmic enzymes that use free Co2+.
摘要
酵母甲硫氨酸氨肽酶I（MetAP I）是酿酒酵母中负责起始甲硫氨酸共翻译切割的两种酶之一。在之前研究的所有原核和真核形式中，它都被归类为一种Co2+金属蛋白酶。然而，用12.5微摩尔/升的Zn2+处理重组脱辅基MetAP I会产生一种酶，其活性与用200微摩尔/升Co2+重构的酶相当。在生理浓度的还原型谷胱甘肽（GSH）存在下，Co-MetAP I无活性，而Zn-MetAP I的活性比在无GSH条件下测定的Zn-MetAP I增加了1.7倍以上。鉴于体内Zn2+的浓度比Co2+至少高1000倍，且Co2+在生理浓度的GSH中不溶，酵母MetAP I实际上可能是一种Zn2+金属蛋白酶。此外，除非存在尚未确定的特殊条件将它们与这种还原环境隔离开或使其与之隔离，否则不太可能存在任何使用游离Co2+的细胞质酶。
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