Substrate-induced inactivation of the Escherichia coli AmiD N-acetylmuramoyl-L-alanine amidase highlights a new strategy to inhibit this class of enzyme

Antimicrobial Agents and Chemotherapy

Volumn 53, Issue 7, 2009, Pages 2991-2997

  Pennartz, Anne ^a   Généreux, Catherine ^a   Parquet, Claudine ^b   Mengin Lecreulx, Dominique ^b   Joris, Bernard ^a,c  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

^c NONE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; CYSTEINE; EDETIC ACID; GLYCOSYLTRANSFERASE; MURAMIC ACID; N ACETYLMURAMOYLALANINE AMIDASE; PEPTIDOGLYCAN; PROTEIN AMIA; PROTEIN AMIB; PROTEIN AMIC; PROTEIN AMID; PROTEINASE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BACTERIAL MEMBRANE; CELL CYCLE; CYTOPLASM; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME KINETICS; ENZYME LOCALIZATION; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; PEPTIDOGLYCAN; SUBSTRATE SPECIFICITY;

EID: 67649994325     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01520-07     Document Type: Article

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