Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase

Biochemistry

Volumn 36, Issue 19, 1997, Pages 5624-5632

  Vanoni, Maria A ^a   Cosma, Antonio ^a   Mazzeo, Daniela ^a   Mattevi, Andrea ^b   Todone, Flavia ^b   Curti, Bruno ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID OXIDASE; DEXTRO AMINO ACID;

AMINO ACID METABOLISM; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; PRIORITY JOURNAL; PROTEIN DEGRADATION; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ALANINE; AMINO ACIDS; ANIMALS; BENZOATES; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; D-AMINO-ACID OXIDASE; DEUTERIUM; FLAVIN-ADENINE DINUCLEOTIDE; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; SUBSTRATE SPECIFICITY; SWINE; TRYPSIN;

EID: 0031010615     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi963023s     Document Type: Article

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