Neutron structure of the T26H mutant of T4 phage lysozyme provides insight into the catalytic activity of the mutant enzyme and how it differs from that of wild type

Author:

Hiromoto Takeshi1,Meilleur Flora23,Shimizu Rumi4,Shibazaki Chie4,Adachi Motoyasu4,Tamada Taro4,Kuroki Ryota1

Affiliation:

1. Quantum Beam Science Center, Japan Atomic Energy Agency; Tokai Ibaraki 319-1195 Japan

2. Neutron Sciences Directorate, Oak Ridge National Laboratory; Oak Ridge Tennessee 37831

3. Department of Molecular and Structural Biochemistry; North Carolina State University; Raleigh North Carolina 27695

4. Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology; Tokai Ibaraki 319-1106 Japan

Funder

MEXT

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference38 articles.

1. Lysozyme-catalyzed hydrolysis and transglycosylation reactions of bacterial cell wall oligosaccharides;Chipman;J Biol Chem,1968

2. Mutational analysis of glycosylase function;Svensson;J Biotechnol,1993

3. Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs;Wohlkönig;PLoS One,2010

4. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate;Vocadlo;Nature,2001

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