The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site

EMBO Journal

Volumn 19, Issue 16, 2000, Pages 4204-4215

  Pawelek, Peter D ^a   Cheah, Jaime ^a   Coulombe, Rene ^a   Macheroux, Peter ^b   Ghisla, Sandro ^c   Vrielink, Alice ^d  

^a MCGILL UNIVERSITY   (Canada)

^b ETH ZURICH   (Switzerland)

^c UNIVERSITY OF KONSTANZ   (Germany)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Crystal structure; Flavoenzyme; Glycosylation; Inhibitor complex; L amino acid oxidase

Indexed keywords

AMINO ACID OXIDASE; ARGININE; BENZOIC ACID DERIVATIVE; CITRIC ACID; GLYCINE;

ARTICLE; ENANTIOMER; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; SEQUENCE HOMOLOGY; SNAKE;

CALLOSELASMA RHODOSTOMA; MAMMALIA; SERPENTES;

EID: 0034663814     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.16.4204     Document Type: Article

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