An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode

Biochemical Journal

Volumn 446, Issue 3, 2012, Pages 405-413

  Larsen, Nicholas A ^a   Nash, Tory J ^a   Morningstar, Marshall ^a   Shapiro, Adam B ^a   Joubran, Camil ^a   Blackett, Carolyn J ^a   Patten, Arthur D ^a   Boriack Sjodin, P Ann ^a   Doig, Peter ^a  

^a ASTRAZENECA   (United Kingdom)

Author keywords

Aminoquinazoline; Cell wall biosynthesis; GlmU; High throughput screening; Inhibitor; Kinase; N acetylglucosamine 1 phosphate uridyltransferase

Indexed keywords

BACTERIAL ENZYME; GLMU ENZYME; QUINAZOLINE DERIVATIVE; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

ARTICLE; BACTERIAL CELL WALL; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DRUG STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; HAEMOPHILUS INFLUENZAE; HYDROPHOBICITY; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

ACETYLGLUCOSAMINE; ACETYLTRANSFERASES; BACTERIAL PROTEINS; BINDING SITES; CELL WALL; CRYSTALLOGRAPHY, X-RAY; HAEMOPHILUS INFLUENZAE; MODELS, MOLECULAR; MULTIENZYME COMPLEXES; NUCLEOTIDYLTRANSFERASES; QUINAZOLINES; STRUCTURE-ACTIVITY RELATIONSHIP; URIDINE TRIPHOSPHATE;

BACTERIA (MICROORGANISMS); HAEMOPHILUS INFLUENZAE;

EID: 84865589369     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120596     Document Type: Article

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