Structure-function relationships in class CA1 cysteine peptidase propeptides.

Abstract:

:Regulation of proteolytic enzyme activity is an essential requirement for cells and tissues because proteolysis at a wrong time and location may be lethal. Proteases are synthesized as inactive or less active precursor molecules in order to prevent such inappropriate proteolysis. They are activated by limited intra- or intermolecular proteolysis cleaving off an inhibitory peptide. These regulatory proenzyme regions have attracted much attention during the last decade, since it became obvious that they harbour much more information than just triggering activation. In this review we summarize the structural background of three functions of clan CA1 cysteine peptidase (papain family) proparts, namely the selectivity of their inhibitory potency, the participation in correct intracellular targeting and assistance in folding of the mature enzyme. Today, we know more than 500 cysteine peptidases of this family from the plant and animal kingdoms, e.g. papain and the lysosomal cathepsins L and B. As it will be shown, the propeptide functions are determined by certain structural motifs conserved over millions of years of evolution.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Wiederanders B

doi

035003691

subject

Has Abstract

pub_date

2003-01-01 00:00:00

pages

691-713

issue

3

eissn

0001-527X

issn

1734-154X

journal_volume

50

pub_type

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