Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
Studies on the specificity of action of bacteriophage T4 lysozyme.
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T4 lysozyme acts as an endo-acetylmuramidase
"T4 acts as an endo-acetylmuramidase capable of cleaving glycosidic bonds only at muramic acid residues that are substituted with peptide side-chains."
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Cleaves glycosidic bonds only at muramic acid residues substituted with peptide side-chains
"cleaving glycosidic bonds only at muramic acid residues that are substituted with peptide side-chains"
Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase.
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This paper characterizes T7 lysozyme, not T4 lysozyme - incorrectly cited for T4 gene E
"Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase"
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T7 lysozyme is an amidase (cleaves peptide-glycan bond), distinct from T4 muramidase
"N-acetylmuramyl-L-alanine amidase"
Purification of bacteriophage T4 lysozyme.
A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme.
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Structural evidence for catalytic mechanism
"The mutation of threonine 26 to glutamic acid in the active site cleft of phage T4 lysozyme (T4L) produced an enzyme that cleaved the cell wall of Escherichia coli but left the product covalently bound to the enzyme"
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T26H mutant traps covalent intermediate
"analysis of its structure showed a covalent linkage between the product and the newly introduced glutamic acid 26. The covalently linked sugar ring was substantially distorted"
Protein determinants of phage T4 lysis inhibition.
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Function of endolysin in lysis pathway
"lysis inhibition in bacteriophage T4 infections occurs when the RI antiholin inhibits the lethal hole-forming function of the T holin"
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Interaction with holin and antiholin system
"the interaction of the soluble domains of these two proteins within the periplasm was necessary for lysis inhibition...Incubation of RI with T inhibits this aggregation and results in a complex of equimolar T and RI content"