title: Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme.
abstract: The amino-terminal structure of rat gastric cathepsin E was identified and compared with the corresponding regions of human procathepsin E and other aspartic proteinases. The alignment revealed that cathepsin E has the most extended amino-terminal structure in aspartic proteinases, thus suggesting that the activation peptide (propeptide) of the human enzyme is 39-residues long. Analysis of oligosaccharide units suggested that rat cathepsin E possesses one N-linked carbohydrate unit, probably of the high mannose type. No evidence was obtained for the presence of O-linked sugars in rat cathepsin E.
authors.affiliation: Department of Zoology, Faculty of Science, Hokkaido University, Sapporo, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Yonezawa
authors.forename: T
authors.initials: T
authors.lastname: Takahashi
authors.forename: M
authors.initials: M
authors.lastname: Ichinose
authors.forename: K
authors.initials: K
authors.lastname: Miki
authors.forename: J
authors.initials: J
authors.lastname: Tanaka
authors.forename: S
authors.initials: S
authors.lastname: Gasa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020059:Cathepsin E; D002403:Cathepsins; D004792:Enzyme Precursors; D006023:Glycoproteins; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006596:Hexosaminidases / Q000494:pharmacology; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats
chemical_list: D004792:Enzyme Precursors; D006023:Glycoproteins; D006026:Glycoside Hydrolases; D006596:Hexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D002403:Cathepsins; D020059:Cathepsin E