Lytic activity of the staphylolytic Twort phage endolysin CHAP domain is enhanced by the SH3b cell wall binding domain

FEMS Microbiology Letters

Volumn 362, Issue 1, 2015, Pages

  Becker, Stephen C ^a   Swift, Steven ^a   Korobova, Olga ^b   Schischkova, Nina ^b   Kopylov, Pavel ^b   Donovan, David M ^a   Abaev, Igor ^b  

^a AGRICULTURAL RESEARCH SERVICE   (United States)

^b STATE RESEARCH CENTER FOR APPLIED MICROBIOLOGY AND BIOTECHNOLOGY   (Russian Federation)

Author keywords

autolysin; bacteriophage endolysin; peptidoglycan hydrolase; Staphylococcus aureus

Indexed keywords

CALCIUM; CYSTEINE; EDETIC ACID; HISTIDINE; HYDROLASE; MAGNESIUM; MANGANESE; PEPTIDASE; ZINC; DIVALENT CATION; ENDOLYSIN; ENZYME ACTIVATOR; PROTEIN BINDING; PROTEINASE;

ARTICLE; BACTERIAL CELL WALL; BACTERIOLYSIS; BACTERIOPHAGE; BACTERIOPHAGE TWORT ENDOLYSIN; BINDING SITE; CHELATION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CYTOLYSIS; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; TURBIDITY; CELL WALL; ENZYMOLOGY; GENE DELETION; GENETICS; HYDROLYSIS; METABOLISM; PROTEIN TERTIARY STRUCTURE; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS PHAGE; VIROLOGY;

BACTERIOLYSIS; CALCIUM; CATIONS, DIVALENT; CELL WALL; ENDOPEPTIDASES; ENZYME ACTIVATORS; HYDROLYSIS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS PHAGES;

EID: 84948430866     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1093/femsle/fnu019     Document Type: Article

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