Engineering of halophilic enzymes: Two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases

Protein Science

Volumn 17, Issue 9, 2008, Pages 1603-1610

  Tokunaga, Hiroko ^a   Arakawa, Tsutomu ^b   Tokunaga, Masao ^a  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b ALLIANCE PROTEIN LABORATORIES   (United States)

Author keywords

Halomonas; Halophilic; Negative charge; Nucleoside diphosphate kinase; Reversibility; Solubility; Stability

Indexed keywords

ALANINE; AMINO ACID; GLUTAMIC ACID; NUCLEOSIDE DIPHOSPHATE KINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPARATIVE STUDY; ENZYME ANALYSIS; ENZYME ENGINEERING; HALOMONAS; PRIORITY JOURNAL; PSEUDOMONAS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACIDS, ACIDIC; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME STABILITY; ESCHERICHIA COLI; HALOMONAS; HOT TEMPERATURE; ISOELECTRIC POINT; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MUTATION; NUCLEOSIDE-DIPHOSPHATE KINASE; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN RENATURATION; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS; SODIUM CHLORIDE; SOLUBILITY; TIME FACTORS;

HALOMONAS; HALOMONAS SP. #593; PSEUDOMONAS;

EID: 50049123899     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.035725.108     Document Type: Article

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