Directed evolution by accumulating tailored mutations: Thermostabilization of lactate oxidase with less trade-off with catalytic activity

Protein Engineering, Design and Selection

Volumn 19, Issue 11, 2006, Pages 483-489

  Hamamatsu, Norio ^a   Nomiya, Yukiko ^a   Aita, Takuyo ^b   Nakajima, Motowo ^a   Husimi, Yuzuru ^b   Shibanaka, Yasuhiko ^a  

^a NOVARTIS PHARMA K K   (Japan)

^b SAITAMA UNIVERSITY   (Japan)

Author keywords

Additivity principles; Directed evolution; Lactate oxidase; Local fitness landscape; Thermostability

Indexed keywords

CATALYST ACTIVITY; THERMODYNAMIC STABILITY;

ADDITIVITY PRINCIPLES; DIRECTED EVOLUTION; LACTATE OXIDASE; LOCAL FITNESS LANDSCAPE; THERMOSTABILITY;

ENZYME KINETICS;

LACTATE 2 MONOOXYGENASE; MUTANT PROTEIN;

AEROCOCCUS VIRIDANS; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; EVOLUTION; HALF LIFE TIME; MUTAGENESIS; MUTATIONAL ANALYSIS; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; RISK REDUCTION; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; DIRECTED MOLECULAR EVOLUTION; ENZYME STABILITY; HALF-LIFE; KINETICS; MIXED FUNCTION OXYGENASES; MUTAGENESIS, SITE-DIRECTED; PEPTIDE LIBRARY; POLYMERASE CHAIN REACTION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; STREPTOCOCCACEAE; THERMODYNAMICS;

EID: 33750353815     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzl034     Document Type: Article

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