Role of lysine versus arginine in enzyme cold-adaptation: Modifying lysine to homo-arginine stabilizes the cold-adapted α-amylase from Pseudoalteramonas haloplanktis

Proteins: Structure, Function and Genetics

Volumn 64, Issue 2, 2006, Pages 486-501

  Siddiqui, Khawar Sohail ^a   Poljak, Anne ^a   Guilhaus, Michael ^a   De Francisci, Davide ^a   Curmi, Paul M G ^a,b   Feller, Georges ^c   D'Amico, Salvino ^c   Gerday, Charles ^c   Uversky, Vladimir N ^d,e,f   Cavicchioli, Ricardo ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b ST VINCENT S HOSPITAL   (Australia)

^c UNIVERSITY OF LIÈGE   (Belgium)

^d INDIANA UNIVERSITY   (United States)

^e INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

^f Molecular Kinetics Inc   (United States)

Author keywords

Bioinformatics; Enzyme kinetics; Guanidination; Psychrophilic; Structure function stability relationship; Thermodynamics

Indexed keywords

AMYLASE; ARGININE; GUANIDINE; LYSINE;

ARTICLE; COLD ACCLIMATIZATION; ENZYME STABILITY; ENZYME STRUCTURE; GEL ELECTROPHORESIS; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; PSEUDOALTERAMONAS HALOPLANKTIS; PSEUDOALTEROMONAS; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

ALPHA-AMYLASE; AMINO ACID SEQUENCE; ANIMALS; COLD; HOMOARGININE; HUMANS; LYSINE; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PSEUDOALTEROMONAS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SWINE;

PSEUDOALTEROMONAS HALOPLANKTIS;

EID: 33745609527     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20989     Document Type: Article

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