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See detailBacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics
Ghuysen, Jean-Marie ULg; Frère, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Scandinavian Journal of Infectious Diseases (1984), 42

Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a ... [more ▼]

Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a set of DD-peptidases which utilize this D-Ala-D-Ala dipeptide--once it has been translocated at the outer face of the plasma membrane as the C-terminal portion of a disaccharide peptide unit--as carbonyl donor for transpeptidation and carboxypeptidation reactions (without additional energy expenditure). Four DD-peptidases have been selected which differ from each other with respect to the effects that amino compounds exert on the fate and rate of consumption of a D-Ala-D-Ala terminated amide carbonyl donor analogue. They serve as models to understand the different mechanisms by which the DD-peptidases perform catalysis and show widely varying responses to the action of beta-lactams, from extreme sensitivity to very high resistance. [less ▲]

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See detailOn the Active Centers of Serine and Zn II DD-carboxyppetidases
Charlier, Paulette ULg; Coyette, Jacques ULg; Dideberg, Otto et al

in Gregory, G.I. (Ed.) Recent advances in the Chemistry of beta-lactam antibiotics (1980)

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See detailInteraction between penicillin and its enzyme target
Ghuysen, Jean-Marie ULg; Frère, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Microbial Drug Resistance : Mechanism, Epidemiology, & Disease (1979), 2

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See detailFractionation of the DD-carboxypeptidase-transpeptidase activities solubilized from membranes of Escherichia coli K12, strain 44
Pollock, Jerry J.; Nguyen-Disteche, Martine; Ghuysen, Jean-Marie ULg et al

in European Journal of Biochemistry (1974), 41(3), 439-446

A transpeptidase activity in Escherichia coli was measured independently of other enzymes involved in peptidoglycan synthesis by quantitating the formation of UDP-N-acetylmuramyl-l-alanyl-y-d-glutamyl-(l ... [more ▼]

A transpeptidase activity in Escherichia coli was measured independently of other enzymes involved in peptidoglycan synthesis by quantitating the formation of UDP-N-acetylmuramyl-l-alanyl-y-d-glutamyl-(l)-meso-diaminopimelyl-(l)-d-alanyl-[14C]glycine when UDP-N-acetylmuramyl-l-alanyl-y-d-glutamyl-(l)-meso-diaminopimelyl-(l-d-alanyl-d-alanine was used as donor substrate and [14C]glycine as acceptor in a transfer reaction. After extraction of membrane envelopes with Brij-36T and subsequent ammonium sulfate precipitation, DEAE-cellulose chromatography revealed two major fractions; one not adsorbed to the ion-exchange resin and the other adsorbed. The fraction which was bound to DEAE-cellulose was bound to and could be eluted from an ampicillin affinity chromatography system while the fraction not bound to DEAE-cellulose was also not bound to the ampicillin column. Both unbound and bound ampicillin fractions exhibited dd-carboxypeptidase and transpeptidase activities although for equivalent dd-carboxypeptidase activity, the bound ampicillin fraction required about five times more glycine acceptor to achieve the same amount of transpeptidation as the unbound ampicillin fraction. [less ▲]

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See detailStructure of the cell wall of Staphylococcus aureus, strain Copenhagen. IX. Teichoic acid and phage adsorption
Coyette, Jacques ULg; Ghuysen, Jean-Marie ULg

in Biochemistry (1968), 7(6), 2385-2389

Selective degradation of the teichoic acid and the peptidoglycan polymers of the walls of Staphylococcus aureus (Copenhagen) by several defined techniques shows that 4-O-β-(N-acetyl-D-glucosaminyl ... [more ▼]

Selective degradation of the teichoic acid and the peptidoglycan polymers of the walls of Staphylococcus aureus (Copenhagen) by several defined techniques shows that 4-O-β-(N-acetyl-D-glucosaminyl) substitution of the D-ribitol units of the teichoic acid moiety is essential to phage fixation and that, in order to be operative, these groups must possess a definite configuration which, in the native walls, is imparted by the binding of the teichoic acid to the supporting peptidoglycan. [less ▲]

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