Insights into the slow-onset tight-binding inhibition of Escherichia coli dihydrofolate reductase: Detailed mechanistic characterization of pyrrolo [3,2-f] quinazoline-1,3-diamine and its derivatives as novel tight-binding inhibitors

FEBS Journal

Volumn 282, Issue 10, 2015, Pages 1922-1938

  Srinivasan, Bharath ^a   Skolnick, Jeffrey ^a  

^a GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

dihydrofolate reductase; drug discovery; mechanistic characterization; pyrrolo 3,2 f quinazoline 1,3 diamine; slow tight binding inhibition

Indexed keywords

7 [(4 AMINOPHENYL)METHYL] 7H PYRROLO [3,2 F]QUINAZOLINE 1,3 DIAMINE; 7H PYRROLO [3,2 F]QUINAZOLINE 1,3 DIAMINE; DIAMINE DERIVATIVE; DIHYDROFOLATE REDUCTASE; DIHYDROFOLIC ACID; METHOTREXATE; UNCLASSIFIED DRUG; DIAMINE; ENZYME INHIBITOR; PROTEIN BINDING;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DRUG BINDING; DRUG POTENCY; DRUG STRUCTURE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; ESCHERICHIA COLI; HUMAN; INHIBITION KINETICS; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; DRUG EFFECTS; ENZYMOLOGY; METABOLISM;

ESCHERICHIA COLI; PROKARYOTA;

DIAMINES; ENZYME INHIBITORS; ESCHERICHIA COLI; PROTEIN BINDING; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 84929582841     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13244     Document Type: Article

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