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Peer-reviewed veterinary case report

The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain.

Journal:
Applied and environmental microbiology
Year:
2006
Authors:
Donovan, David M et al.
Affiliation:
Biotechnology and Germplasm Laboratory · United States

Abstract

The Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. Truncations and point mutations indicated that the Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity.

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Original publication: https://pubmed.ncbi.nlm.nih.gov/16820517/