Benzimidazole analogs of l-tryptophan are substrates and inhibitors of tryptophan indole lyase from Escherichia coli

FEBS Journal

Volumn 280, Issue 8, 2013, Pages 1807-1817

  Harris, Austin P ^a   Phillips, Robert S ^a,b  

^a UNIVERSITY OF GEORGIA   (United States)

^b University of Georgia   (United States)

Author keywords

elimination; enzyme mechanism; pyridoxal 5 phosphate; steady state kinetics; stopped flow kinetics

Indexed keywords

2 AMINO 4 (BENZIMIDAZOL 1 YL)PROPIONIC ACID; 2 AMINO 5 (BENZIMIDAZOL 1 YL)PENTANOIC ACID; 3 BENZIMIDAZOL 1 YL ALANINE; BENZIMIDAZOLE DERIVATIVE; DEHYDROALANINE; DIAMINE; LYASE; QUINONE DERIVATIVE; TRYPTOPHAN; TRYPTOPHAN INDOLE LYASE; UNCLASSIFIED DRUG;

ARTICLE; COMPETITIVE INHIBITION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG DESIGN; DRUG STRUCTURE; ENZYME BINDING; ENZYME INHIBITION; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; SPECTROPHOTOMETRY; STEADY STATE;

BENZIMIDAZOLES; ENZYME INHIBITORS; ESCHERICHIA COLI; KINETICS; TRYPTOPHAN; TRYPTOPHANASE;

ENTEROBACTERIACEAE; ESCHERICHIA COLI;

EID: 84876292015     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12205     Document Type: Article

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