The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity

Journal of Biological Chemistry

Volumn 281, Issue 19, 2006, Pages 13762-13776

  Lohkamp, Bernhard ^a   Andersen, Birgit ^b   Piškur, Jure ^b   Dobritzsch, Doreen ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; HYDROLYSIS; SUBSTRATES; THREE DIMENSIONAL; YEAST; ZINC;

PHYSIOLOGICALLY RELEVANT; PYRIMIDINE DEGRADATIONS; SANDWICH DOMAINS; STEREOSELECTIVITY;

ENZYMES;

ALANINE; AMIDASE; CARBAMYL BETA ALANINE; DIHYDROOROTASE; DIHYDROPYRIMIDINASE; DIHYDROURACIL; PROTEIN SUBUNIT; TETRAMER; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DICTYOSTELIUM DISCOIDEUM; ENZYME SPECIFICITY; NERVE CELL DIFFERENTIATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; SACCHAROMYCES; SACCHAROMYCES KLUYVERI;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DICTYOSTELIUM; DIMERIZATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; SACCHAROMYCES; SUBSTRATE SPECIFICITY; THYMINE; URACIL;

DICTYOSTELIUM DISCOIDEUM; EUKARYOTA; SACCHAROMYCES KLUYVERI;

EID: 33744961438     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M513266200     Document Type: Article

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