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
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:45 p.m.
|Number of data points||18|
|Proteins||Endolysin ; Endolysin|
|Assays/Quantities/Protocols||Experimental Assay: dG ; Experimental Assay: Tm ; Experimental Assay: dHvH ; Derived Quantity: ddG ; Derived Quantity: dTm|
|Libraries||Mutations for sequence MVEINNQRKAFLDMLAWSEGTDNGRQKTRNHGYDVIVGGELFTDYSDHPRKLVTLNPKLKSTGAGRYQLLSRWWDAYRKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGGTVREIDV|
|Percent Identity||Matching Chains||Protein||Accession||Entry Name|