Modulation of the electrostatic charge at the active site of foot-and-mouth-disease-virus leader proteinase, an unusual papain-like enzyme

Biochemical Journal

Volumn 363, Issue 3, 2002, Pages 493-501

  Schlick, Petra ^a   Kronovetr, Jakub ^a   Hampoelz, Bernhard ^a   Skern, Tim ^a  

^a UNIVERSITY OF VIENNA   (Austria)

Author keywords

Cysteine proteinase; Enzyme mechanism; Ion pair; RNA virus; Translation initiation

Indexed keywords

BIOSYNTHESIS; DISEASES; ELECTROSTATICS; ENZYMES; MUTAGENESIS; POLYPEPTIDES; VIRUSES;

CELLULAR SUBSTRATE;

BIOCHEMISTRY;

ALANINE; AMINO ACID; ASPARAGINE; ASPARTIC ACID; HEXAPEPTIDE; INITIATION FACTOR 4G; LYSINE; MUTANT PROTEIN; PAPAIN; PROLINE; PROTEINASE; SERINE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME MECHANISM; FOOT AND MOUTH DISEASE VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; REACTION TIME; SITE DIRECTED MUTAGENESIS; TRANSLATION INITIATION;

AMINO ACID SUBSTITUTION; ASPARAGINE; ASPARTIC ACID; BINDING SITES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ELECTROSTATICS; ENDOPEPTIDASES; ESCHERICHIA COLI; EUKARYOTIC INITIATION FACTOR-4G; FOOT-AND-MOUTH DISEASE VIRUS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PAPAIN; PEPTIDE INITIATION FACTORS; SERINE;

EUKARYOTA; FOOT-AND-MOUTH DISEASE VIRUS; ORYCTOLAGUS CUNICULUS; RNA VIRUSES;

EID: 0036565773     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3630493     Document Type: Article

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