title: Purification and primary structure determination of human lysosomal dipeptidase.
abstract: The lysosomal metallopeptidase is an enzyme that acts preferentially on dipeptides with unsubstituted N- and C-termini. Its activity is highest in slightly acidic pH. Here we describe the isolation and characterization of lysosomal dipeptidase from human kidney. The isolated enzyme has the amino-terminal sequence DVAKAIINLAVY and is a homodimer with a molecular mass of 100 kDa. So far no amino acid sequence has been determined for this metallopeptidase. The complete primary structure as deduced from the nucleotide sequence revealed that the isolated dipeptidase is similar to blood plasma glutamate carboxypeptidase.
authors.affiliation: Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, Sl-1000 Ljubljana, Slovenia.
authors.forename: Iztok
authors.initials: I
authors.lastname: Dolenc
authors.forename: Marko
authors.initials: M
authors.lastname: Mihelic
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019281:Dimerization; D004150:Dipeptidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D006801:Humans; D007668:Kidney / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D017386:Sequence Homology, Amino Acid
chemical_list: D004150:Dipeptidases; C038937:dipeptidase