Reference : Histidine modification and mutagenesis point to the involvement of a large conformationa...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/64079
Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme
English
Evrard, Christine mailto [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Biochimie Physique et des Biopolymères > >]
Fastrez, Jacques mailto [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Biochimie Physique et des Biopolymères > >]
Soumillion, Patrice mailto [Université Catholique de Louvain - UCL > Département de Chimie > Laboratoire de Biochimie Physique et des Biopolymères > >]
1999
FEBS Letters
Elsevier Science
460
442-446
Yes (verified by ORBi)
International
0014-5793
Amsterdam
The Netherlands
[en] Lysozyme ; Diethyl pyrocarbonate ; Functional motion
[en] Phage lambda lysozyme is structurally related to other known lysozymes but its mechanism of action is different from the classical lysozyme mechanism, acting as a transglycosidase rather than a hydrolase. As two conformations have been revealed by the crystal structure, we investigated the effect of mutating and modifying a histidine located near to or far from the active site in the respective closed and open conformations. Whereas its asparagine mutation has little or no effect on activity, its N-carbethoxylation inactivates the enzyme. This provide further evidence for the involvement of the closed conformation and for the need of conformational mobility in lambda lysozyme function.
http://hdl.handle.net/2268/64079
http://www.elsevier.com/wps/find/journaldescription.cws_home/506085/description#description

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