Balancing the stability and the catalytic specificities of OP hydrolases with enhanced V-agent activities

Protein Engineering, Design and Selection

Volumn 21, Issue 6, 2008, Pages 405-412

  Reeves, T E ^a,b   Wales, M E ^a   Grimsley, J K ^a   Li, P ^a   Cerasoli, D M ^b   Wild, J R ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b US ARMY MEDICAL RESEARCH INSTITUTE OF CHEMICAL DEFENSE   (United States)

Author keywords

Cation interactions; Chemical warfare agents; Organophosphorus hydrolase; Protein stability; Rational design

Indexed keywords

AGENTS; CHEMICAL WARFARE; INITIATORS (CHEMICAL); MICROFLUIDICS; MILITARY OPERATIONS; STABILIZERS (AGENTS); SYSTEM STABILITY;

AGENT ACTIVITIES; CATALYTIC ACTIVITIES; CHEMICAL WARFARE AGENTS (CWA); GENETICALLY MODIFIED (GM); HYDROLASES; ORGANOPHOSPHORUS HYDROLASE (OPH); SITE DIRECTED MUTAGENESIS; TURNOVER NUMBER (TON);

THERMODYNAMIC STABILITY;

AMINO ACID; ARYLDIALKYLPHOSPHATASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME MODIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURAL PROTEOMICS; THERMODYNAMICS; THERMOSTABILITY; WILD TYPE; X RAY CRYSTALLOGRAPHY;

ARYLDIALKYLPHOSPHATASE; CATALYSIS; CHEMICAL WARFARE AGENTS; ENZYME STABILITY; HYDROLYSIS; MODELS, MOLECULAR; ORGANOTHIOPHOSPHORUS COMPOUNDS; PROTEIN CONFORMATION; PROTEIN DENATURATION;

EID: 44649197217     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzn019     Document Type: Article

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