A weak dd-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli

FEMS Microbiology Letters

Volumn 303, Issue 1, 2010, Pages 76-83

  Chowdhury, Chiranjit ^a   Nayak, Tapas R ^a   Young, Kevin D ^b   Ghosh, Anindya S ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

^b UNIVERSITY OF ARKANSAS FOR MEDICAL SCIENCES   (United States)

Author keywords

Dd carboxypeptidase; Escherichia coli; Morphology maintenance; Penicillin binding proteins

Indexed keywords

BETA LACTAM ANTIBIOTIC; BOCILLIN FL; CARBOXYPEPTIDASE; HYBRID PROTEIN; KANAMYCIN; PENICILLIN BINDING PROTEIN 5; PENICILLIN DERIVATIVE; PENICILLIN G; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BETA LACTAM; ESCHERICHIA COLI PROTEIN; PENICILLIN BINDING PROTEIN; PROTEIN BINDING;

ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; NUCLEOTIDE SEQUENCE; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; ULTRAVIOLET SPECTROSCOPY; CELL WALL; CHEMICAL STRUCTURE; CYTOLOGY; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETIC COMPLEMENTATION; GENETICS; HYDROLYSIS; METABOLISM; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; ANTI-BACTERIAL AGENTS; BETA-LACTAMS; CARBOXYPEPTIDASES; CATALYTIC DOMAIN; CELL WALL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENETIC COMPLEMENTATION TEST; HYDROLYSIS; MODELS, MOLECULAR; PENICILLIN-BINDING PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 74349093311     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2009.01863.x     Document Type: Article

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