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A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein.

Abstract：

:Pepsin, a gastric aspartic proteinase, is a zymogen-derived protein that undergoes irreversible alkaline denaturation at pH 6-7. Detailed knowledge of the structure of the alkaline-denatured state is an important step in understanding the mechanism of the formation of the active enzyme. An extensive analysis of the denatured state at pH 8.0 was performed using a variety of techniques including (1)H nuclear magnetic resonance spectroscopy and solution X-ray scattering. This analysis indicates that the denatured state under these conditions has a compact and globular conformation with a substantial amount of secondary and tertiary structures. The data suggest that this partially structured species has a highly folded region and a flexible region. The NMR measurements suggest that the folded region contains His53 and is located at least partly in the N-terminal lobe of the protein. The alkaline-denatured state experiences a further reversible denaturation step at higher pH or on heating; the midpoints of the unfolding transition are pH 11.5 (at 25 degrees C) and 53.1 degrees C (at pH 8.0), respectively. The present findings suggest that the proteolytic processing of pepsinogen has substantially modified the ability of the protein to fold, such that its folding process cannot progress beyond the partially folded intermediate of pepsin.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Konno T,Kamatari YO,Tanaka N,Kamikubo H,Dobson CM,Nagayama K

doi

10.1021/bi991923d

subject

Has Abstract

pub_date

2000-04-11 00:00:00

pages

4182-90

issue

14

eissn

0006-2960

issn

1520-4995

pii

bi991923d

journal_volume

39

pub_type

杂志文章

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