Antimicrobial Peptides Released by Enzymatic Hydrolysis of Hen Egg White Lysozyme

2004 ◽  
Vol 52 (5) ◽  
pp. 1088-1094 ◽  
Author(s):  
Yoshinori Mine ◽  
Fupeng Ma ◽  
Sophie Lauriau
1996 ◽  
Vol 315 (2) ◽  
pp. 473-479 ◽  
Author(s):  
Paul G. RICHARDS ◽  
David J. WALTON ◽  
John HEPTINSTALL

We have investigated the effects of tyrosine nitration (to form the weak acid, 3-nitrotyrosine) at positions 23 or 20 plus 23, on the structure and function of hen egg-white lysozyme. Enzyme activity against Micrococcus luteus cell-wall fragments or soluble substrates exhibits two phenomena. (a) A decrease in Km and kcat for the hydrolysis of soluble oligo- and poly-saccharides, resulting in only minor changes in the catalytic efficiency (kcat/Km) upon nitration. (b) The hydrolysis of M. luteus cell-wall fragments appeared to be dominated by electrostatic interactions with the protein, giving a decrease in enzyme activity as the 3-nitrotyrosyl group became ionized. Removal of the cell-wall anionic polymer, teichuronic acid, from M. luteus abolished this effect. The 3-nitrotyrosine group was also found to act as a fluorescence quencher of exposed tryptophan residues in lysozyme.


2014 ◽  
Vol 136 ◽  
pp. 73-80 ◽  
Author(s):  
Karen Stroobants ◽  
Phuong Hien Ho ◽  
Eva Moelants ◽  
Paul Proost ◽  
Tatjana N. Parac-Vogt

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu

Sign in / Sign up

Export Citation Format

Share Document