Autocatalytic processing of procathepsin E to cathepsin E and their structural differences.

Abstract:

:The processing of human gastric procathepsin E to its mature form, cathepsin E, was studied at pH 3.5. The results revealed the autocatalytic and apparently one-step conversion of procathepsin E to cathepsin E within 10 min of incubation at 14 degrees C under the conditions used. Analyses of the amino acid sequences of both procathepsin E and cathepsin E showed that cleavage occurred at the Met36-Ile37 bond to produce the mature form, cathepsin E. The NH2-terminal amino acid sequence of procathepsin E thus determined was identical with that predicted from the cDNA sequence by Azuma et al. except that the NH2-terminal glutamine residue in the latter was converted into a pyroglutamic acid residue in the former and that the glycine residue at position 2 in the latter sequence was deleted in the former. On the other hand, the NH2-terminal amino acid sequence of cathepsin E was identical with that reported previously by us.

authors

Athauda SB,Takahashi T,Kageyama T,Takahashi K

doi

10.1016/s0006-291x(05)81213-6

subject

Has Abstract

pub_date

1991-02-28 00:00:00

pages

152-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)81213-6

journal_volume

175

pub_type

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