RGD Reference Report - Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression. - Rat Genome Database

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Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression.

Authors: Fukasawa, K  Fukasawa, KM  Kanai, M  Fujii, S  Hirose, J  Harada, M 
Citation: Fukasawa K, etal., Biochem J 1998 Jan 15;329 ( Pt 2):275-82.
RGD ID: 728641
Pubmed: PMID:9425109   (View Abstract at PubMed)
PMCID: PMC1219041   (View Article at PubMed Central)

We have purified dipeptidyl peptidase III (EC 3.4.14.4) from human placenta. It had a pH optimum of 8.8 and readily hydrolysed Arg-Arg-beta-naphthylamide. Monoamino acid-, Gly-Phe-, Gly-Pro- and Bz-Arg-beta-naphthylamides were not hydrolysed at all. The enzyme was inhibited by p-chloromercuriphenylsulphonic acid, metal chelators and 3,4-dichloroisocoumarin and contained 1 mol of zinc per mol of enzyme. The zinc dissociation constant was 250 fM at pH 7. 4 as determined by the zinc binding study. We isolated, by immunological screening of a Uni-ZAP XR cDNA library constructed from rat liver mRNA species, a cDNA clone with 2633 bp encoding the rat enzyme. The longest open reading frame encodes a 827-residue protein with a theoretical molecular mass of 92790 Da. Escherichia coli SOLR cells were infected with the pBluescript phagemid containing the cloned cDNA and established the overexpression of a protein that hydrolysed Arg-Arg-beta-naphthylamide. The recombinant protein was purified and the amino acid sequence of the protein was confirmed. We presumed that the putative zinc-binding domain involved in catalysis was present in the recombinant enzyme. It was a novel zinc-binding motif in that one amino acid residue was inserted into the conserved HEXXH motif characteristic of the metalloproteinases.

Objects referenced in this article
Gene Dpp3 dipeptidylpeptidase 3 Rattus norvegicus

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