Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme.


Abstract

Phage lambda lysozyme (lambdaL) 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 lambdaL function. Study holds ProTherm entries: 14587, 14588, 14589, 14590, 14591, 14592, 14593, 14594 Extra Details: lysozyme; diethyl pyrocarbonate; functional motion

Submission Details

ID: vsZguSvb

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:45 p.m.

Version: 1

Publication Details
Evrard C;Fastrez J;Soumillion P,FEBS Lett. (1999) Histidine modification and mutagenesis point to the involvement of a large conformational change in the mechanism of action of phage lambda lysozyme. PMID:10556513
Additional Information

Sequence Assay Result Units