Tryptophan 243 affects interprotein contacts, cofactor binding and stability in D-amino acid oxidase from Rhodotorula gracilis

FEBS Journal

Volumn 273, Issue 3, 2006, Pages 504-512

  Caldinelli, Laura ^a   Molla, Gianluca ^a   Pilone, Mirella S ^a   Pollegioni, Loredano ^a  

^a UNIVERSITY OF INSUBRIA   (Italy)

Author keywords

Cofactor binding; Flavoprotein; Oligomerization state; Rational design; Structural stability

Indexed keywords

APOPROTEIN; DEXTRO AMINO ACID OXIDASE; ISOLEUCINE; MONOMER; TRYPTOPHAN; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CATALYST; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; RHODOTORULA; TEMPERATURE DEPENDENCE; WILD TYPE;

D-AMINO-ACID OXIDASE; ELECTROSTATICS; ENZYME ACTIVATION; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RHODOTORULA; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE; TIME FACTORS; TRYPTOPHAN; UREA;

RHODOSPORIDIUM TORULOIDES;

EID: 33644957672     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.05083.x     Document Type: Article

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