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The role of the N-terminal propeptide of the pro-aminopeptidase processing protease: refolding, processing, and enzyme inhibition.

Abstract：

:Pro-aminopeptidase processing protease (PA protease) is an extracellular zinc metalloprotease produced by Aeromonas caviae T-64 and it is classified as M04.016 according to the MEROPS database. The precursor of PA protease consists of four regions; a signal peptide, an N-terminal propeptide, a C-terminal propeptide, and the mature PA protease. The in vitro refolding of the intermediate pro-PA protease containing the C-terminal propeptide (MC) was investigated in the presence and absence of the N-terminal propeptide. The results indicate that the noncovalently linked N-terminal propeptide is able to assist in the refolding of MC. In the absence of the N-terminal propeptide, MC is trapped into a folding competent state that is converted into the active form by the addition of the N-terminal propeptide. Moreover, the N-terminal propeptide was found to form a complex with the folded MC and inhibit further processing of MC into the mature PA protease. Inhibitory activity of the purified N-terminal propeptide toward mature PA protease was also observed, and the mode of this inhibition was determined to be a mixed, noncompetitive inhibition with an associated allosteric effect.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tang B,Nirasawa S,Kitaoka M,Hayashi K

doi

10.1016/s0006-291x(02)00838-0

subject

Has Abstract

pub_date

2002-08-09 00:00:00

pages

78-84

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006291X02008380

journal_volume

296

pub_type

杂志文章

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