Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E.
The amino acid sequences in the NH2-terminal region and some other parts of human gastric cathepsin E were investigated. The NH2-terminal sequencing revealed that the cathepsin E preparation which had been activated at pH 4.0 contained one major and one minor isozymes in an approximate molar ratio of 3:1. The NH2-terminal sequence of the former was very similar to but partly different from that predicted from cDNA sequencing by Azuma et al., whereas the latter had an NH2-terminal sequence identical with the predicted sequence. These results provide structural evidence for the presence of at least two isozymic forms in human gastric cathepsin E. In addition, the site of carbohydrate attachment was elucidated by isolation and analysis of a glycopeptide fraction from an enzymatic digest of cathepsin E. A single carbohydrate chain was deduced to be attached to the asparagine residue at position 34 in the major isozyme and to the corresponding asparagine residue in the minor isozyme.
Athauda
S B
SB
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Matsuzaki
O
O
Kageyama
T
T
Takahashi
K
K
D000595:Amino Acid Sequence; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002241:Carbohydrates; D020059:Cathepsin E; D002403:Cathepsins / Q000235:genetics; D004247:DNA / Q000235:genetics; D005753:Gastric Mucosa / Q000201:enzymology*; D006801:Humans; D007527:Isoenzymes / Q000235:genetics; D008969:Molecular Sequence Data
D002241:Carbohydrates; D007527:Isoenzymes; D004247:DNA; D002403:Cathepsins; D020059:Cathepsin E