The structure of L-hydantoinase from Arthobacter aurescens leads to an understanding of dihydropyrimidinase substrate and enantio specificity

Biochemistry

Volumn 41, Issue 27, 2002, Pages 8589-8597

  Abendroth, Jan ^a,b   Niefind, Karsten ^a   May, Oliver ^c   Siemann, Martin ^c   Syldatk, Christoph ^c   Schomburg, Dietmar ^a  

^a UNIVERSITY OF COLOGNE   (Germany)

^b UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF STUTTGART   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLOYTIC ACTIVITY;

AMINO ACIDS; BIOTECHNOLOGY; CATALYSIS; SUBSTRATES;

ENZYMES;

DIHYDROOROTASE; DIHYDROPYRIMIDINASE; DIHYDROPYRIMIDINE; PHOSPHOTRIESTERASE; PYRIMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTHROBACTER; ARTHROBACTER AURESCENS; ARTICLE; BIOTECHNOLOGY; CATABOLISM; ENANTIOMER; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; IMAGE ANALYSIS; NONHUMAN; OPTICAL RESOLUTION; PRIORITY JOURNAL; RACEMIC MIXTURE; STEREOCHEMISTRY; THERMUS; THREE DIMENSIONAL IMAGING;

AMIDOHYDROLASES; ARTHROBACTER; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

ACTINOBACTERIA (CLASS); ARTHROBACTER; ARTHROBACTER AURESCENS; THERMUS; THERMUS SP.; UNCULTURED ACTINOMYCETE;

EID: 0037046968     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0157722     Document Type: Article

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