Department of Physiology and Biochemistry, University of Malta, Msida, MSD2080, Malta.
Institute of Earth Systems, University of Malta, Msida, MSD2080, Malta.
Chemistry. 2018 Apr 6;24(20):5303-5308. doi: 10.1002/chem.201704655. Epub 2017 Dec 12.
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.
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。