scholarly journals Disintegrin-like/cysteine-rich domains of the reprolysin HF3: Site-directed mutagenesis reveals essential role of specific residues

Biochimie ◽  
2011 ◽  
Vol 93 (2) ◽  
pp. 345-351 ◽  
Author(s):  
Milene C. Menezes ◽  
Ana Karina de Oliveira ◽  
Robson L. Melo ◽  
Mônica Lopes-Ferreira ◽  
Vanessa Rioli ◽  
...  
1997 ◽  
Vol 328 (2) ◽  
pp. 343-347 ◽  
Author(s):  
Luis MATA ◽  
Marta ERRA-PUJADA ◽  
Jean-Claude GRIPON ◽  
Michel-Yves MISTOU

PepCs isolated from lactic acid bacteria and bleomycin hydrolases of eukaryotic organisms are strict aminopeptidases which belong to the papain family of thiol peptidases. The structural basis of the enzymic specificity of the lactococcal PepC has been investigated by site-directed mutagenesis. The deletion of the C-terminal residue (Ala-435) abolished the aminopeptidase activity, whereas this deletion led to a new peptidase specificity. The enzymic properties of wild-type and mutant PepCs demonstrate that the terminal α-carboxy group plays a key role in the strict aminopeptidase activity.


1992 ◽  
Vol 267 (36) ◽  
pp. 25754-25758
Author(s):  
J Wu ◽  
D Filer ◽  
A.J. Friedhoff ◽  
M Goldstein

1990 ◽  
Vol 265 (20) ◽  
pp. 11788-11795
Author(s):  
K D Egeberg ◽  
B A Springer ◽  
S G Sligar ◽  
T E Carver ◽  
R J Rohlfs ◽  
...  

Biochemistry ◽  
2005 ◽  
Vol 44 (42) ◽  
pp. 13970-13980 ◽  
Author(s):  
Barbara Cellini ◽  
Mariarita Bertoldi ◽  
Riccardo Montioli ◽  
Carla Borri Voltattorni

Sign in / Sign up

Export Citation Format

Share Document