{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Varotsou C"],"funding":["Hellenic Foundation for Research and Innovation"],"pagination":["8523"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10218239"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(10)"],"pubmed_abstract":["The emergence of multidrug-resistant (MDR) bacteria has risen rapidly, leading to a great threat to global public health. A promising solution to this problem is the exploitation of phage endolysins. In the present study, a putative N-acetylmuramoyl-L-alanine type-2 amidase (NALAA-2, EC 3.5.1.28) from <i>Propionibacterium</i> bacteriophage PAC1 was characterized. The enzyme (<i>Pa</i>Ami1) was cloned into a T7 expression vector and expressed in <i>E. coli</i> BL21 cells. Kinetics analysis using turbidity reduction assays allowed the determination of the optimal conditions for lytic activity against a range of Gram-positive and negative human pathogens. The peptidoglycan degradation activity of <i>Pa</i>Ami1 was confirmed using isolated peptidoglycan from <i>P. acnes</i>. The antibacterial "],"journal":["International journal of molecular sciences"],"pubmed_title":["Characterization and Engineering Studies of a New Endolysin from the <i>Propionibacterium acnes</i> Bacteriophage PAC1 for the Development of a Broad-Spectrum Artilysin with Altered Specificity."],"pmcid":["PMC10218239"],"funding_grant_id":["4036"],"pubmed_authors":["Labrou NE","Premetis GE","Varotsou C"],"additional_accession":[]},"is_claimable":false,"name":"Characterization and Engineering Studies of a New Endolysin from the <i>Propionibacterium acnes</i> Bacteriophage PAC1 for the Development of a Broad-Spectrum Artilysin with Altered Specificity.","description":"The emergence of multidrug-resistant (MDR) bacteria has risen rapidly, leading to a great threat to global public health. A promising solution to this problem is the exploitation of phage endolysins. In the present study, a putative N-acetylmuramoyl-L-alanine type-2 amidase (NALAA-2, EC 3.5.1.28) from <i>Propionibacterium</i> bacteriophage PAC1 was characterized. The enzyme (<i>Pa</i>Ami1) was cloned into a T7 expression vector and expressed in <i>E. coli</i> BL21 cells. Kinetics analysis using turbidity reduction assays allowed the determination of the optimal conditions for lytic activity against a range of Gram-positive and negative human pathogens. The peptidoglycan degradation activity of <i>Pa</i>Ami1 was confirmed using isolated peptidoglycan from <i>P. acnes</i>. The antibacterial ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-04-07T17:35:56.055Z","creation":"2024-11-21T02:00:38.813Z"},"accession":"S-EPMC10218239","cross_references":{"pubmed":["37239874"],"doi":["10.3390/ijms24108523"]}}