Metal-binding and active-site structure of di-zinc Streptomyces griseus aminopeptidase

Abstract

 Streptomyces griseus aminopeptidase has been characterized to have a dinuclear active site and to follow a dinuclear hydrolytic mechanism by means of activity assay, optical, and NMR spectroscopy. A sequential binding of Co2+ to the dinuclear sites in 20 mM Mes buffer at pH 6.1 has also been established. The results from these studies suggest that the two metal sites have a five-coordination sphere, with at least one coordinated His each. A di-Cu2+-substituted derivative of the enzyme has been prepared which exhibits a 1H NMR spectrum with sharp hyperfine-shifted signals, again indicating the presence of a dinuclear active site. This 1H NMR spectrum with sharp hyperfine-shifted features represents a first of its kind for a di-Cu2+ center in metalloproteins.

DOI: 10.1007/s007750050190

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Cite this paper

@article{Lin1997MetalbindingAA, title={Metal-binding and active-site structure of di-zinc Streptomyces griseus aminopeptidase}, author={Lung-Yu Lin and Hyun Ik Park and L Ming}, journal={JBIC Journal of Biological Inorganic Chemistry}, year={1997}, volume={2}, pages={744-749} }