Importance of the hydrogen bonding network including Asp52 for catalysis, as revealed by Asn59 mutant hen egg-white lysozymes

Journal of Biochemistry

Volumn 146, Issue 5, 2009, Pages 651-657

  Ose, Toyoyuki ^a   Kuroki, Kimiko ^a   Matsushima, Masaaki ^b   Maenaka, Katsumi ^a   Kumagai, Izumi ^c  

^a KYUSHU UNIVERSITY   (Japan)

^b AINO UNIVERSITY   (Japan)

^c TOHOKU UNIVERSITY   (Japan)

Author keywords

Catalytic activity; Lysozyme; Protein engineering; Proteincarbohydrate interactions; X ray crystallography

Indexed keywords

ASPARAGINE; ASPARTIC ACID; CARBENE; EGG WHITE; GLUTAMINE; LYSOZYME; N ACETYLGLUCOSAMINE;

ARTICLE; BACTERIOLYSIS; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME BINDING; FEMALE; HEN; HYDROGEN BOND; HYDROLYSIS; MOLECULAR INTERACTION; MUTANT; NONHUMAN; SURFACE CHARGE; WILD TYPE;

ACETYLGLUCOSAMINE; ANIMALS; ASPARTIC ACID; BACTERIOLYSIS; BIOCATALYSIS; CATALYTIC DOMAIN; CHICKENS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; HYDROLYSIS; MURAMIDASE; MUTANT PROTEINS; MYCOBACTERIUM; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 70449627525     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp110     Document Type: Article

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