Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme.
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.
Yonezawa
S
S
Department of Zoology, Faculty of Science, Hokkaido University, Sapporo, Japan.
Takahashi
T
T
Ichinose
M
M
Miki
K
K
Tanaka
J
J
Gasa
S
S
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
D004792:Enzyme Precursors; D006023:Glycoproteins; D006026:Glycoside Hydrolases; D006596:Hexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D002403:Cathepsins; D020059:Cathepsin E