3C-like Proteinase from SARS Coronavirus Catalyzes Substrate Hydrolysis by a General Base Mechanism

Biochemistry

Volumn 43, Issue 15, 2004, Pages 4568-4574

  Huang, Changkang ^a   Wei, Ping ^a   Fan, Keqiang ^a   Liu, Ying ^a   Lai, Luhua ^a,b  

^a PEKING UNIVERSITY   (China)

^b PEKING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; HYDROLYSIS; ISOTOPES; MUTAGENESIS; PH EFFECTS; REACTION KINETICS;

DRUG DESIGN; ENZYME CATALYTIC MECHANISM; PROTEINASE; SARS;

ENZYMES;

3C LIKE PROTEINASE; ALANINE; BASE; CHYMOTRYPSIN; CYSTEINE; CYSTEINE PROTEINASE; DEUTERIUM OXIDE; HISTIDINE; IMIDAZOLE DERIVATIVE; ISOTOPE; PAPAIN; SERINE; THIOL DERIVATIVE; UNCLASSIFIED DRUG; VIRUS ENZYME;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CATALYST; COLORIMETRY; ENTHALPY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; NONHUMAN; PH; PKA; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; SARS CORONAVIRUS;

ALANINE; AMINO ACID SUBSTITUTION; CATALYSIS; COLORIMETRY; CYSTEINE; CYSTEINE ENDOPEPTIDASES; DEUTERIUM EXCHANGE MEASUREMENT; ENDOPEPTIDASES; HISTIDINE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MUTAGENESIS, SITE-DIRECTED; SARS VIRUS; SERINE; SOLVENTS; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMODYNAMICS; VIRAL PROTEINS;

CORONAVIRUS; RNA VIRUSES; SARS CORONAVIRUS;

EID: 3142613358     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036022q     Document Type: Article

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