scholarly journals Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli.

1975 ◽  
Vol 72 (9) ◽  
pp. 3428-3432 ◽  
Author(s):  
J. Rouviere-Yaniv ◽  
F. Gros
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Low Molecular Weight

scholarly journals Purification and Characterization of PBP4a, a New Low-Molecular-Weight Penicillin-Binding Protein fromBacillus subtilis

2001 ◽  
Vol 183 (5) ◽  
pp. 1595-1599 ◽  
Author(s):  
Colette Duez ◽  
Marc Vanhove ◽  
Xavier Gallet ◽  
Fabrice Bouillenne ◽  
Jean-Denis Docquier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Binding Protein ◽  
Order Rate Constant ◽  
Low Molecular Weight ◽  
Penicillin Binding Protein ◽  
Purification And Characterization ◽  
The Third

ABSTRACT Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits dd-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frère, and J. M. Ghuysen, Biochem. J. 282:781–788, 1992), which is rapidly inactivated by many β-lactams, PBP4a is only moderately sensitive to these compounds. The second-order rate constant (k 2/K) for the acylation of the essential serine by benzylpenicillin is 300,000 M−1s−1 for the Actinomadura sp. strain R39 peptidase, 1,400 M−1 s−1 for B. subtilis PBP4a, and 7,000 M−1 s−1 forEscherichia coli PBP4, the third member of this class of PBPs. Cephaloridine, however, efficiently inactivates PBP4a (k 2/K = 46,000 M−1 s−1). PBP4a is also much more thermostable than the R39 enzyme.

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