Foot-and-mouth disease virus leader proteinase: a papain-like enzyme requiring an acidic environment in the active site.

Abstract:

:Foot-and-mouth disease virus leader proteinase (L(pro)), a papain-like cysteine proteinase, has six acidic amino acids between 4 A and 11 A of the catalytic dyad of Cys51 and His148. In contrast, in papain and related enzymes, only one acidic residue lies within this distance. We have examined by site-directed mutagenesis the importance of each of these residues for L(pro) self-processing and cleavage of its cellular substrate, eukaryotic initiation factor 4GI. Only substitution of the electrostatic charge of aspartate 164 affected enzyme activity. Thus, in contrast to the prototype papain, L(pro) activity requires a negative charge 4.5 A from the catalytic dyad.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kronovetr J,Skern T

doi

10.1016/s0014-5793(02)03237-4

keywords:

subject

Has Abstract

pub_date

2002-09-25 00:00:00

pages

58-62

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302032374

journal_volume

528

pub_type

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