Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologues

Journal of Biochemistry

Volumn 142, Issue 4, 2007, Pages 539-552

  Suadee, Chutintorn ^a   Nijvipakul, Sarayut ^a   Svasti, Jisnuson ^a   Entsch, Barrie ^b,c   Ballou, David P ^b   Chaiyen, Pimchai ^a  

^a MAHIDOL UNIVERSITY   (Thailand)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF NEW ENGLAND   (Australia)

Author keywords

Bioluminescence; Flavin; Luciferase; Monooxygenase; Vibrio campbellii

Indexed keywords

LUCIFERASE; FLAVINE MONONUCLEOTIDE;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; BIOLUMINESCENCE; CATALYSIS; ENZYME BINDING; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; MOLECULAR CLONING; PH MEASUREMENT; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; STRUCTURAL HOMOLOGY; TEMPERATURE DEPENDENCE; THERMALLY STIMULATED LUMINESCENCE; THERMOSTABILITY; VIBRIO; VIBRIO CAMPBELLII; VIBRIO HARVEYI; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PHOTOBACTERIUM; PHYSIOLOGY; PROTEIN BINDING; THERMODYNAMICS;

ESCHERICHIA COLI; VIBRIO CAMPBELLII;

AMINO ACID SEQUENCE; BASE SEQUENCE; ENZYME STABILITY; FLAVIN MONONUCLEOTIDE; KINETICS; LUCIFERASES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PHOTOBACTERIUM; PROTEIN BINDING; STRUCTURAL HOMOLOGY, PROTEIN; THERMODYNAMICS; VIBRIO;

EID: 38449118003     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm155     Document Type: Article

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