A conserved surface loop in type i dehydroquinate dehydratases positions an active site arginine and functions in substrate binding

Biochemistry

Volumn 50, Issue 12, 2011, Pages 2357-2363

  Light, Samuel H ^a   Minasov, George ^a   Shuvalova, Ludmilla ^a   Peterson, Scott N ^a,b   Caffrey, Michael ^c   Anderson, Wayne F ^a   Lavie, Arnon ^c  

^a NORTHWESTERN UNIVERSITY   (United States)

^b J CRAIG VENTER INSTITUTE   (United States)

^c UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CONFORMATIONAL CHANGE; DEHYDROQUINATE; DIRECT INTERACTIONS; LIGAND BINDING; LOOP CONFORMATION; PATHOGENIC BACTERIUM; SALMONELLA ENTERICA; SHIKIMATE PATHWAY; SIDE CHAINS; STRUCTURAL STUDIES; SUBSTRATE BINDING; SURFACE LOOPS; WILD TYPES;

ARGININE; BACTERIA; CONFORMATIONS; SUBSTRATES;

AMINO ACIDS;

AMINO ACID; ARGININE; DEHYDROQUINATE DEHYDRATASE; LYASE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BINDING AFFINITY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; LIGAND BINDING; PRIORITY JOURNAL; SALMONELLA ENTERICA;

AMINO ACID SEQUENCE; ARGININE; BIOCATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; HYDRO-LYASES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING; SALMONELLA ENTERICA;

SALMONELLA ENTERICA;

EID: 79952925947     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi102020s     Document Type: Article

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