Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase: A site-directed mutagenesis study

European Journal of Biochemistry

Volumn 269, Issue 19, 2002, Pages 4762-4771

  Boselli, Angelo ^a   Sacchi, Silvia ^a   Job, Viviana ^a   Pilone, Mirella S ^a   Pollegioni, Loredano ^a  

^a UNIVERSITY OF INSUBRIA   (Italy)

Author keywords

Active site lid; Flavoprotein; Function structure relationships; Reaction mechanism; Substrate recognition

Indexed keywords

ACRIFLAVINE; CARBOXYLIC ACID; DEXTRO ALANINE; DEXTRO AMINO ACID OXIDASE; MUTANT PROTEIN; PHENYLALANINE; SEMIQUINONE; SERINE; TYROSINE;

ARTICLE; BINDING ASSAY; CATALYST; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; LIGAND BINDING; MOLECULAR INTERACTION; OXIDATION REDUCTION REACTION; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; RHODOTORULA; SITE DIRECTED MUTAGENESIS; TURNOVER TIME;

ALANINE; CATALYTIC DOMAIN; D-AMINO-ACID OXIDASE; KINETICS; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION; RHODOTORULA; SPECTROPHOTOMETRY; SUBSTRATE SPECIFICITY; TYROSINE;

RHODOSPORIDIUM TORULOIDES; TRIXIS;

EID: 0036400659     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.t01-1-03173.x     Document Type: Article

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