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[51] Exocellular dd-carboxypeptidases-transpeptidases from Streptomyces
Frère, Jean-Marie; Leyh-Bouille, Mélina; Ghuysen, Jean-Marie et al.
1976In Lorand, Laszlo (Ed.) Part B: Proteolytic Enzymes
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Keywords :
amino acids/analysis; carboxypeptidases/isolation & purification/metabolism; cephalosporins; kinetics; methods; molecular weight; muramoylpentapeptide carboxypeptidase/isolation & purification/metabolism; penicillinase/metabolism; penicillins; protein conformation; spectrophotometry; streptomyces/*enzymology; structure-activity relationship
Abstract :
[en] Strains R39 and R61 are soil isolates. Their designations are arbitrary. In strain R39, the cross-link between the peptide units of the wall peptidoglycan extends from the C-terminal D-alanine of one unit to the amino group at the D-center of meso-diaminopimelic acid of another unit (peptidoglycan of chemotype I). The interpeptide bond is in position to a free carboxyl group. In strain R61, the cross-link extends from a C-terminal D-alanine of a peptide unit to a glycine residue attached to the amino group of LL-diaminopimelic acid of another peptide unit (peptidoglycan of chemotype II). The exocellular DD carboxypeptidases-transpeptidases produced by both strains catalyze hydrolysis, react with β-lactam antibiotics. This chapter explains the assay methods for DD-Carboxypeptidase activity like the standard reaction, chemical estimation of free Alanine, as well as, assay method for β-Lactamase. It also discusses the Excretion of DD-Carboxypeptidase-Transpeptidase and β -Lactamase by Streptomyces R39, Excretion of DD-Carboxypeptidase-Transpeptidase and β-Lactamase by Streptomyces R61, purification of the DD-Carboxypeptidase-Transpeptidase from Streptomyces R39 (for 500 Liters of Culture Fluid), Purification of the DD-Carboxypeptidase-Transpeptidase from Streptomyces R61 (for 400 Liters of Culture Fluid), Physicochemical Properties of DD-Carboxypeptidases-Transpeptidases from Streptomyces R39 and R61, Interaction between DD-Carboxypeptidases-Transpeptidases from Streptomyces R39 and R61 and β-Lactam Antibiotics , Titration of DD-Carboxypeptidases-Transpeptidases from Streptornyces R39 and R61 by β-Lactam Antibiotics, Hydrolysis Reactions Catalyzed by the DD-Carboxypeptidases-Transpeptidases from Streptomyces R39 and R61, Concomitant Hydrolysis and Transfer Reactions Involving Distinct Donor and Acceptor Peptides, Catalyzed by the DD-Carboxypeptidases-Transpeptidases from Streptonayces R39 and R61, Concomitant Hydrolysis and Transfer Reactions Catalyzed by the DD-Carboxypeptidases-Transpeptidases from Streptomyces R39 and R61 and in Which the Same Peptide Acts as Donor and Acceptor and Inhibition of DD-Carboxypeptidases-Transpeptidases from Streptomyces R39 and R61 by β-Lactam Antibiotics in the Presence of Substrates. Copyright © 1976 Published by Elsevier Inc.
Disciplines :
Microbiology
Biochemistry, biophysics & molecular biology
Author, co-author :
Frère, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie
Leyh-Bouille, Mélina;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de microbiologie
Nieto, Manuel
Perkins, Harold R.
Language :
English
Title :
[51] Exocellular dd-carboxypeptidases-transpeptidases from Streptomyces
Publication date :
01 January 1976
Main work title :
Part B: Proteolytic Enzymes
Editor :
Lorand, Laszlo
Publisher :
Academic Press
ISBN/EAN :
978-0-12-181945-3
Collection name :
Methods in Enzymology. vol. 45
Pages :
610-636
Peer reviewed :
Peer reviewed
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