Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases. - Wikidata - awgldk - TriplyDB

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

http://www.wikidata.org/entity/Q34693872

about

Glycosyltransferases and Transpeptidases/Penicillin-Binding Proteins: Valuable Targets for New Antibacterials Some properties of a D-alanine carboxypeptidase in envelope fractions of Neisseria gonorrhoeae Penicillin-resistant temperature-sensitive mutants of Escherichia coli which synthesize hypo- or hyper-cross-linked peptidoglycan.Transpeptidase-mediated incorporation of D-amino acids into bacterial peptidoglycan.DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.Exocellular beta-lactamases of Streptomyces albus G and strains R39 and K11 beta-Lactamase-catalyzed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptors Reactions of peptidoglycan-mimetic beta-lactams with penicillin-binding proteins in vivo and in membranes Isolation by covalent affinity chromatography of the penicillin-binding components from membranes of Bacillus subtilis.Lipoprotein activators stimulate Escherichia coli penicillin-binding proteins by different mechanisms.Distinct pathways for modification of the bacterial cell wall by non-canonical D-amino acids Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.Mode of action of glycine on the biosynthesis of peptidoglycan.Fluorescence and circular dichroism studies on the Streptomyces R61 DD-carboxypeptidase-transpeptidase. Penicillin binding by the enzyme Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39.Reconstitution of peptidoglycan cross-linking leads to improved fluorescent probes of cell wall synthesis.The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties Detection of lipid-linked peptidoglycan precursors by exploiting an unexpected transpeptidase reaction.Peptide inhibitors of Streptomyces DD-carboxypeptidases.Membrane-bound DD-carboxypeptidases from Bacillus megaterium KM general properties, substrate specificity and sensitivity to penicillins, cephalosporins and peptide inhibitors of the activity at pH5.Molecular weight and amino acid composition of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of streptomyces R61.Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.The direction of peptide trimer synthesis from the donor-acceptor substrate Nalpha-(acetyl)-Nepsilon-(glycyl)-L-lysyl-D-alanyl-D-alanine by the exocellular dd-carboxypeptidase-transpeptidase of Streptomyces R61.The penicillin receptor in Streptomyces.

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P2860

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

http://www.wikidata.org/entity/Q34693872

description

1972 nî lūn-bûn

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1972 թուականի Մարտին հրատարակուած գիտական յօդուած

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1972 թվականի մարտին հրատարակված գիտական հոդված

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1972年の論文

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1972年論文

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1972年論文

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1972年論文

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1972年論文

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1972年論文

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1972年论文

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name

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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type

label

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

@en

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

@en

P2093

Frere JM

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Ghuysen JM

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Johnson K

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Leyh-Bouille M

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Linder R

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Nieto M

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Salton MR

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P2860

Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.

Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.

Studies on the acceptor specificity of the lysozyme-catalyzed transglycosylation reaction.

The specificity of combination between ristocetins and peptides related to bacterial cell wall mucopeptide precursors.

Structure of the meso-diaminopimelic acid containing peptidoglycans in Escherichia coli B and Bacillus megaterium KM.

Peptidoglycan synthesis in bacilli. II. Characteristics of protoplast membrane preparations.

LL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A).

Biosynthesis of the peptidoglycan of bacterial cell walls. 8. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of Escherichia coli.

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662-666

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10.1073/PNAS.69.3.662

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3

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69

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