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Literature summary for 3.2.1.17 extracted from

  • Donovan, D.M.; Foster-Frey, J.; Dong, S.; Rousseau, G.M.; Moineau, S.; Pritchard, D.G.
    The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain (2006), Appl. Environ. Microbiol., 72, 5108-5112.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Streptococcus phage B30
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidoglycan + H2O the Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. The Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity Streptococcus phage B30 ?
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Synonyms

Synonyms Comment Organism
endolysin
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Streptococcus phage B30