Effects of subsite alterations on substrate-binding mode in the active site of hen egg-white lysozyme |
| |
Authors: | I Kumagai K Maenaka F Sunada S Takeda K Miura |
| |
Affiliation: | ERS 20 CNRS (Phylogénie moléculaire des Annélides), Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France. |
| |
Abstract: | The primary sequence of the low-molecular-mass cadmium-binding protein metalloprotein II of Nereis diversicolor (Hediste diversicolor, recent denomination) has been determined. This protein is composed of 119 amino acids and has 80.8% identity with the N. diversicolor myohemerythrin [Takagi, T. & Cox, J. A. (1991) FEBS Lett. 285, 25-27]. The fact that iron, which normally binds to myohemerythrin, is not found to be associated with the cadmium-binding protein metalloprotein II in cadmium-exposed animals could be the result of the complete abolition of the iron-binding capacity of the protein due to the binding of cadmium. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|