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

FEBS Letters

Skern, Tim¹  Kronovetr, Jakub¹ 

[1]Institute for Medical Biochemistry, Division of Biochemistry, University of Vienna, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria

关键词: Papain-like cysteine proteinase;    Active site;    Foot-and-mouth disease virus;    Leader proteinase;    Electrostatic interactions;    Initiation of translation;    eIF4G;    eukaryotic initiation factor 4GI;    FMDV;    foot-and-mouth disease virus;    Lpro;    leader proteinase;    RRL;    rabbit reticulocyte lysate;   

DOI  :  10.1016/S0014-5793(02)03237-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Foot-and-mouth disease virus leader proteinase (L^pro), a papain-like cysteine proteinase, has six acidic amino acids between 4 Å and 11 Å 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 Å from the catalytic dyad.

【 授权许可】

Unknown