scholarly journals Purification and characterization of a glycine betaine binding protein from Escherichia coli.

1987 ◽  
Vol 262 (24) ◽  
pp. 11841-11846
Author(s):  
A Barron ◽  
J U Jung ◽  
M Villarejo
Keyword(s):  
Escherichia Coli ◽  
Glycine Betaine ◽  
Binding Protein ◽  
Purification And Characterization

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.

Purification and Characterization of the Periplasmic Nickel-Binding Protein NikA of Escherichia coli K12

1995 ◽  
Vol 227 (3) ◽  
pp. 857-865 ◽  
Author(s):  
Karinne Pina ◽  
Clarisse Navarro ◽  
Laura Mcwalter ◽  
David H. Boxer ◽  
Nicholas C. Price ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Purification And Characterization ◽  
Escherichia Coli K12 ◽  
Nickel Binding

scholarly journals Purification and Characterization of the Periplasmic Nickel-Binding Protein NikA of Escherichia coli K12

2008 ◽  
Vol 227 (3) ◽  
pp. 857-865 ◽  
Author(s):  
Karinne Pina ◽  
Clarisse Navarro ◽  
Laura Mcwalter ◽  
David H. Boxer ◽  
Nicholas C. Price ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Purification And Characterization ◽  
Escherichia Coli K12 ◽  
Nickel Binding

scholarly journals Properties of HflX, an Enigmatic Protein from Escherichia coli

2009 ◽  
Vol 191 (7) ◽  
pp. 2307-2314 ◽  
Author(s):  
Dipak Dutta ◽  
Kaustav Bandyopadhyay ◽  
Ajit Bikram Datta ◽  
Abhijit A. Sardesai ◽  
Pradeep Parrack
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Purification And Characterization ◽  
Gtp Binding Protein ◽  
Functional Roles ◽  
Gtp Binding ◽  
Its Gene ◽  
Coliphage Lambda

ABSTRACT The Escherichia coli gene hflX was first identified as part of the hflA operon, mutations in which led to an increased frequency of lysogenization upon infection of the bacterium by the temperate coliphage lambda. Independent mutational studies have also indicated that the HflX protein has a role in transposition. Based on the sequence of its gene, HflX is predicted to be a GTP-binding protein, very likely a GTPase. We report here purification and characterization of the HflX protein. We also specifically examined its suggested functional roles mentioned above. Our results show that HflX is a monomeric protein with a high (30% to 40%) content of helices. It exhibits GTPase as well as ATPase activities, but it has no role in lambda lysogeny or in transposition.

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