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Iztok Dolenc, Roger Pain, Vito Turk
Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization
Keywords: blood plasma glutamate carboxypeptidase, dipeptidase, dipeptide, expression, folding, lysosomal dipeptidase, lysosome
Lysosomal dipeptidase catalyzes the hydrolysis of dipeptides with unsubstituted terminals. It is a homodimer and binds zinc. Dimerization is an important issue in understanding the enzyme's function. In this study, we investigated the influence of the propeptide on the folding and dimerization of recombinant lysosomal dipeptidase. For this purpose, we separately cloned and overexpressed the mature protein and the proenzyme. The overexpressed proteins were localized exclusively to insoluble inclusion bodies. Refolding of the urea-solubilized inclusion bodies showed that only dipeptidase lacking the propeptide was dimeric. The soluble renatured proenzyme was a monomer, although circular dichroism and fluorescence spectra of the proenzyme indicated the formation of secondary and tertiary structure. The propeptide thus controls dimerization, as well as activation, of lysosomal dipeptidase.
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 388, 01/2007
Pages: 47 - 51