Metal Binding and Active Site Structure of Di-Zinc Streptomyces griseus Aminopeptidase
Lin, L.-Y.; Park, H. I.; Ming, L.-J.*
Department of Chemistry and Institute for Biomolecular Science, University of South Florida, Tampa, FL 33620
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 H-1 NMR spectrum
with sharp hyperfine-shifted signals, again indicating the presence of
a dinuclear active site. This H-1 NMR spectrum with sharp hyperfine-shifted
features represents a first of its kind for a di-Cu2+
center in metalloproteins.
(Read a short introduction about aminopeptidase)
(Read abstract about NMR study of di-Cu(II)-aminopeptidase
from Aeromonas)
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