Succinylphosphonate esters are competitive inhibitors of MenD that show active-site discrimination between homologous α-ketoglutarate- decarboxylating enzymes

Biochemistry

Volumn 49, Issue 12, 2010, Pages 2672-2679

  Fang, Maohai ^a   Daniel Toogood, R ^a   Mácova, Andrea ^a   Ho, Karen ^a   Franzblau, Scott G ^b   McNeil, Michael R ^c   Sanders, David A R ^a   Palmer, David R J ^a  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^c Department of Environmental and Radiological Health Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYLPHOSPHONATE; BINDING CHARACTERISTICS; CATALYTIC PROCESSING; DECARBOXYLATION REACTIONS; HYPOXIC CONDITION; IN-VITRO; KETOGLUTARATE; KETOGLUTARATE DEHYDROGENASE COMPLEXES; M. TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS; SITE-DIRECTED MUTATION; STRUCTURE ACTIVITY RELATIONSHIPS; THIAMIN DIPHOSPHATE-DEPENDENT ENZYMES;

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; CATALYSTS; ENZYMES; ESTERIFICATION; ESTERS;

ENZYME INHIBITION;

2 OXOGLUTARIC ACID; ACYLPHOSPHONATE ESTER; ALANINE; ALPHA KETOGLUTARATE DECARBOXYLATING ENZYME; LYSINE; MENAQUINONE; MEND ENZYME; PHOSPHONIC ACID ESTER; SUCCINYLPHOSPHONATE ESTER; THIAMINE DERIVATIVE; UNCLASSIFIED DRUG;

AEROBIC CAPACITY; ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL GROWTH; BIOSYNTHESIS; CATALYSIS; CHEMICAL STRUCTURE; CONTROLLED STUDY; DECARBOXYLATION; DRUG SYNTHESIS; ENZYME INHIBITION; MUTATIONAL ANALYSIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION;

CATALYTIC DOMAIN; CHORISMIC ACID; ENZYME INHIBITORS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KETOGLUTARATE DEHYDROGENASE COMPLEX; KETOGLUTARIC ACIDS; KINETICS; MUTAGENESIS, SITE-DIRECTED; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THIAMINE PYROPHOSPHATE;

MYCOBACTERIUM TUBERCULOSIS;

EID: 77949796314     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901432d     Document Type: Article

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