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Penicillin binding proteins and model transpeptidase activity of the plasma membranes of Streptomyces strains R61 and rimosus
Dusart, Jean; Reynolds, Peter E.; Ghuysen, Jean-Marie
1981In FEMS Microbiology Letters, 12 (3), p. 299-303
 

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Abstract :
[en] Streptomyces R61 and S. rimosus have an atypical penicillin-binding protein (PBP) pattern characterized by a large amt. of a 25,000-mol.-wt. protein and a small amt. of a 50,000-mol.-wt. protein. The 25,000-mol.-wt. PBP exhibits high thermostability and apparently is the membrane-bound enzyme which catalyzes the model transpeptidase reaction in which Ac2-L-Lys-D-Ala-D-Ala serves as the carbonyl donor and Gly-Gly as the amino acceptor. Whether the thermolabile 50,000-mol.-wt. PBP is also a transpeptidase and is degraded into small fragments or converted into the 25,000-mol.-wt. PBP is unclear. [on SciFinder(R)]
Disciplines :
Microbiology
Author, co-author :
Dusart, Jean;  Université de Liège - ULiège > Institut de Chimie > Service de Micorbiologie
Reynolds, Peter E.;  University of Cambridge > Department of Biochemistry, Sub-Department of Chemical Microbiology
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Chimie > Service de Micorbiologie
Language :
English
Title :
Penicillin binding proteins and model transpeptidase activity of the plasma membranes of Streptomyces strains R61 and rimosus
Publication date :
1981
Journal title :
FEMS Microbiology Letters
ISSN :
0378-1097
eISSN :
1574-6968
Publisher :
Oxford University Press, United Kingdom
Volume :
12
Issue :
3
Pages :
299-303
Available on ORBi :
since 16 September 2011

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