Abstract
Dipeptidyl peptidase III, a metallopeptidase of the M49 family, was first identified (in the pituitary) by its specific cleavage of diarginyl arylamides, which have been used as preferred assay substrates until now. Here we examined the activity of the yeast and human dipeptidyl peptidase III in parallel. The human enzyme preferred Arg2-β-naphthylamide and showed 620-fold higher kcat/Km for this substrate. In contrast, the yeast enzyme did not display a preference for any of the X-Arg-β-naphthylamide analyzed. The replacement of Gly505 with Asp, resulted in a less active, but more selective, yeast enzyme form. These results indicate diversity in cleavage specificity in the M49 family.
Support for this study by the Croatian Ministry of Science, Education and Sport (Project 098-1191344-2938) is gratefully acknowledged.
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Articles in the same Issue
- Masthead
- Masthead
- Reviews
- The unique activity of bone morphogenetic proteins in bone: a critical role of the Smad signaling pathway
- The formate/nitrite transporter family of anion channels
- The human Ah receptor: hints from dioxin toxicities to deregulated target genes and physiological functions
- Heparan sulfate: a key regulator of embryonic stem cell fate
- Research Articles/Short Communications
- Genes and Nucleic Acids
- Expression and translation of the COX-1b gene in human cells – no evidence of generation of COX-1b protein
- Protein Structure and Function
- Evaluation of the metal binding sites in a recombinant coagulation factor VIII identifies two sites with unique metal binding properties
- Hydrolysis of dipeptide derivatives reveals the diversity in the M49 family
- Molecular Medicine
- Betulinic acid suppresses NGAL-induced epithelial-to-mesenchymal transition in melanoma
- Proteolysis
- Influence of partial unfolding and aggregation of human stefin B (cystatin B) EPM1 mutants G50E and Q71P on selective cleavages by cathepsins B and S
- The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine
- Book Review
- Extracellular Matrix: Pathobiology and Signaling