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Foot‐and‐mouth disease virus leader proteinase: a papain‐like enzyme requiring an acidic environment in the active site
Author(s) -
Kronovetr Jakub,
Skern Tim
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03237-4
Subject(s) - papain , enzyme , cysteine , biochemistry , chemistry , active site , site directed mutagenesis , protease , cleavage (geology) , residue (chemistry) , catalytic triad , amino acid , biology , paleontology , fracture (geology) , mutant , gene
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.