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单个突变足以改变真核锰超氧化物歧化酶对铁的金属选择性和特异性。

A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron.

机构信息

Department of Physiology and Biochemistry, University of Malta, Msida, MSD2080, Malta.

Institute of Earth Systems, University of Malta, Msida, MSD2080, Malta.

出版信息

Chemistry. 2018 Apr 6;24(20):5303-5308. doi: 10.1002/chem.201704655. Epub 2017 Dec 12.

Abstract

We have generated a site-directed mutant of the manganese superoxide dismutase SOD-3 of C.elegans (MnSOD-3) which modifies the metal specificity of the enzyme. While wild-type MnSOD-3 functions with manganese in the active site (3600 U mg of protein) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50 % of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron.

摘要

我们已经产生了一种线虫锰过氧化物歧化酶 SOD-3 的定点突变体(MnSOD-3),它改变了酶的金属特异性。虽然野生型 MnSOD-3在活性位点(3600Umg 蛋白)中与锰一起发挥作用,但当铁被掺入时,它几乎没有或没有活性。然而,当活性位点的谷氨酸 142 被组氨酸取代时,该酶保留了其 50%的活性,并变得对其金属辅因子具有兼性,表现出与锰或铁非常相似的比活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7f2a/5969255/cdedaeafdd0a/CHEM-24-5303-g001.jpg

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