The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum

Journal of Biological Chemistry

Volumn 283, Issue 52, 2008, Pages 36553-36563

  Fiuza, Maria ^a   Canova, Marc J ^b   Patin, Delphine ^c   Letek, Michal ^a   Zanella Cléon, Isabelle ^b   Becchi, Michel ^b   Mateos, Luís M ^a   Mengin Lecreulx, Dominique ^c,d   Molle, Virginie ^b   Gil, José A ^a  

^a UNIVERSITY OF LEÓN   (Spain)

^b INSTITUT DE BIOLOGIE ET CHIMIE DES PROTÉINES   (France)

^c UNIVERSITÉ PARIS SACLAY   (France)

^d CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; CHEMICAL REACTIONS; ENZYMES; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NUCLEIC ACIDS; POLYSACCHARIDES;

ACID CONTENTS; ALANINE RESIDUES; ANTIBACTERIALS; BACTERIAL CELLS; CATALYTIC ACTIVITIES; CORYNEBACTERIUM GLUTAMICUM; ENZYMATIC ACTIVITIES; IN-VITRO; IN-VITRO ASSAYS; IN-VIVO; ISOFORM; L ALANINES; LIGASE ACTIVITIES; LIGASES; MASS SPECTROMETRY ANALYSIS; MONOMER UNITS; NUCLEOTIDE PRECURSORS; PEPTIDE MOIETIES; PEPTIDOGLYCAN; PHOSPHORYLATED PROTEINS; PHYSIOLOGICAL MECHANISMS; PROTEIN KINASE; THREONINE RESIDUES;

PHOSPHORYLATION;

LIGASE; MURC LIGASE; PEPTIDOGLYCAN; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CORYNEBACTERIUM GLUTAMICUM; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SYNTHESIS; IN VITRO STUDY; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

ALANINE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DNA PRIMERS; GENE EXPRESSION REGULATION, BACTERIAL; LIGASES; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PEPTIDE SYNTHASES; PEPTIDOGLYCAN; PHOSPHOAMINO ACIDS; PHOSPHORYLATION; PLASMIDS; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); CORYNEBACTERIUM GLUTAMICUM; PROKARYOTA;

EID: 61349099574     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M807175200     Document Type: Article

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