AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae

Nature Communications

Volumn 5, Issue , 2014, Pages

  Klöckner, Anna ^a   Otten, Christian ^a   Derouaux, Adeline ^b,d   Vollmer, Waldemar ^b   Bühl, Henrike ^a   De Benedetti, Stefania ^a   Münch, Daniela ^a   Josten, Michaele ^a   Mölleken, Katja ^c   Sahl, Hans Georg ^a   Henrichfreise, Beate ^a  

^a UNIVERSITY OF BONN   (Germany)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c HEINRICH HEINE UNIVERSITY   (Germany)

^d UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; CARBOXYPEPTIDASE; CARBOXYPEPTIDASE TRANSPEPTIDASE; LIPID; N ACETYLMURAMOYLALANINE AMIDASE; PENICILLIN BINDING PROTEIN; PENICILLIN DERIVATIVE; PEPTIDOGLYCAN; BACTERIAL PROTEIN;

BACTERIUM; CYTOLOGY; ENZYME ACTIVITY; FUNCTIONAL ROLE; INHIBITION; LIPID; PATHOGEN; PHYSIOLOGY; PROTEIN;

ARTICLE; BACTERIAL CELL; BIOSYNTHESIS; CELL DIVISION; CELL WALL; CHLAMYDOPHILA PNEUMONIAE; CONTROLLED STUDY; CYTOKINESIS; DAUGHTER CELL; ENZYME ACTIVITY; ESCHERICHIA COLI; IMMUNE RESPONSE; IMMUNOMODULATION; IN VITRO STUDY; MODULATION; NONHUMAN; AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; CHEMISTRY; CHLAMYDIA PNEUMONIAE; CYTOLOGY; DRUG EFFECTS; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARBOXYPEPTIDASES; CELL WALL; CHLAMYDOPHILA PNEUMONIAE; CYTOKINESIS; MOLECULAR SEQUENCE DATA; PENICILLINS; SEQUENCE ALIGNMENT;

EID: 84903127194     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5201     Document Type: Article

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