Probing mammalian spermine oxidase enzyme–substrate complex through molecular modeling, site-directed mutagenesis and biochemical characterization

Amino Acids ◽  
2010 ◽  
Vol 40 (4) ◽  
pp. 1115-1126 ◽  
Author(s):  
Paraskevi Tavladoraki ◽  
Manuela Cervelli ◽  
Fabrizio Antonangeli ◽  
Giovanni Minervini ◽  
Pasquale Stano ◽  
...  
Author(s):  
Agata Antonina Rita Impellizzeri ◽  
Matteo Pappalardo ◽  
Livia Basile ◽  
Ornella Manfra ◽  
Kjetil Wessel Andressen ◽  
...  

2005 ◽  
Vol 48 (15) ◽  
pp. 4842-4850 ◽  
Author(s):  
Mercedes Martín-Martínez ◽  
Anne Marty ◽  
Maud Jourdan ◽  
Chantal Escrieut ◽  
Elodie Archer ◽  
...  

2004 ◽  
Vol 48 (9) ◽  
pp. 3579-3582 ◽  
Author(s):  
Bibiana Caporale ◽  
Nicola Franceschini ◽  
Mariagrazia Perilli ◽  
Bernardetta Segatore ◽  
Gian Maria Rossolini ◽  
...  

ABSTRACT Three mutants of the extended-spectrum β-lactamase TEM-60, the P51L, K104E, and S164R mutants, were constructed by site-directed mutagenesis. The kinetic parameters of the mutated enzymes and interactions of inhibitors were significantly different from those of TEM-60, revealing that the L51P mutation plays an important role in enzyme activity and stability in the TEM-60 background.


Sign in / Sign up

Export Citation Format

Share Document