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

FEBS Letters

Evrard, Christine¹  Soumillion, Patrice¹  Fastrez, Jacques¹ 

[1] Université Catholique de Louvain, Laboratoire de Biochimie Physique et des Biopolymères, Place L. Pasteur 1–1B, B-1348 Louvain-la-Neuve, Belgium

关键词: Lysozyme;    Diethyl pyrocarbonate;    Functional motion;    DEPC;    diethyl pyrocarbonate;    λL;    T4L;    HEWL;    respectively the lysozymes of lambda;    T4 and hen egg white;   

DOI  :  10.1016/S0014-5793(99)01395-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phage lambda lysozyme (λL) 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 λL function.

【 授权许可】

Unknown