Studies on the reaction mechanism of Rhodotorula gracilis D-amino-acid oxidase. Role of the highly conserved Tyr-223 on substrate binding and catalysis

Journal of Biological Chemistry

Volumn 274, Issue 51, 1999, Pages 36233-36240

  Harris, Christopher M ^a,b   Molla, Gianluca ^b   Pilone, Mirella S ^b   Pollegioni, Loredano ^b  

^a UNIVERSITY OF UTAH   (United States)

^b UNIVERSITY OF INSUBRIA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

DEXTRO AMINO ACID OXIDASE;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; RHODOTORULA; SITE DIRECTED MUTAGENESIS;

BINDING SITES; CATALYSIS; CONSERVED SEQUENCE; D-AMINO-ACID OXIDASE; KINETICS; MUTAGENESIS, SITE-DIRECTED; RHODOTORULA; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TYROSINE;

BACTERIA (MICROORGANISMS); RHODOSPORIDIUM TORULOIDES;

EID: 0033579446     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.51.36233     Document Type: Article

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