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Structural Analysis of an Insect Lysozyme Exhibiting Catalytic Efficiency at Low Temperatures,

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posted on 14.09.2002, 00:00 by Atsushi Matsuura, Min Yao, Tomoyasu Aizawa, Nozomi Koganesawa, Kazuo Masaki, Mitsuhiro Miyazawa, Makoto Demura, Isao Tanaka, Keiichi Kawano, Katsutoshi Nitta
Bombyx mori lysozyme (BmLZ), from the silkworm, is an insect lysozyme. BmLZ has considerable activity at low temperatures and low activation energies compared with those of hen egg white lysozyme (HEWLZ), according to measurements of the temperature dependencies of relative activity (lytic and glycol chitin) and the estimation of activation energies using the Arrhenius equation. Being so active at low temperatures and low activation energies is characteristic of psychrophilic (cold-adapted) enzymes. The three-dimensional structure of BmLZ has been determined by X-ray crystallography at 2.5 Å resolution. The core structure of BmLZ is similar to that of c-type lysozymes. However, BmLZ shows some distinct differences in the two exposed loops and the C-terminal region. A detailed comparison of BmLZ and HEWLZ suggests structural rationalizations for the differences in the catalytic efficiency, stability, and mode of activity between these two lysozymes.