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Literature summary for 3.5.1.28 extracted from

  • Linden, S.; Zhang, H.; Heselpoth, R.; Shen, Y.; Schmelcher, M.; Eichenseher, F.; Nelson, D.
    Biochemical and biophysical characterization of PlyGRCS, a bacteriophage endolysin active against methicillin-resistant Staphylococcus aureus (2015), Appl. Microbiol. Biotechnol., 99, 741-752 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C29S site-directed mutagenesis, catalytically inactive mutant Staphylococcus phage GRCS
H92A site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme Staphylococcus phage GRCS

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Staphylococcus phage GRCS cell walls are treated with enzyme PlyGRCS, revealing that the catalytic activity is an amidase or endopeptidase, PlyGRCS spectrum of lytic activity, overview. The enzyme shows N-acetylmuramoyl-L-alanine amidase activity ?
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?

Organism

Organism UniProt Comment Textmining
Staphylococcus phage GRCS W6E9L0
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information cell walls are treated with enzyme PlyGRCS, revealing that the catalytic activity is an amidase or endopeptidase, PlyGRCS spectrum of lytic activity, overview. The enzyme shows N-acetylmuramoyl-L-alanine amidase activity Staphylococcus phage GRCS ?
-
?

Synonyms

Synonyms Comment Organism
endolysin
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Staphylococcus phage GRCS
GRCS_0011
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Staphylococcus phage GRCS
PlyGRCS
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Staphylococcus phage GRCS

General Information

General Information Comment Organism
additional information enzyme PlyGRCS contains an N-terminal catalytic domain with an active site cysteine and histidine Staphylococcus phage GRCS