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Table 2 Characterisation of proposed phiBIOTICS families of enzybiotics

From: phiBIOTICS: catalogue of therapeutic enzybiotics, relevant research studies and practical applications

phiBIOTICS family Description Pfam family Enzybiotic(s)
Lysozyme Enzymes display lysozyme activity; hydrolyse the (1,4)-β-linkages between N-acetylmuramic acid and N-acetyl-d-glucosamine residues in a peptidoglycan and bonds between N-acetyl-d-glucosamine residues in chitodextrins. Glyco_hydro_25 Cpl-1
Phage B30 lysin
  PlyGBS
CHAP* Phage B30 lysin
    PlyGBS
NAM amidase Enzymes display N-acetylmuramoyl-l-alanine amidase activity; hydrolyse the bond between N-acetylmuramoyl residues and l-amino acid residues in certain bacterial cell-wall glycopeptides. Amidase_2 LysH5
LysK
LytA
MV-L
phi11 endolysin
PlyG
  PlyL
Amidase_3 CD27L
  Ply3626
Amidase_5 Pal
  PlyV12
CHAP* LysH5
LysK
    phi11 endolysin
Other amidase/peptidase Enzymes contain CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) domain. This domain has been proposed to hydrolyse γ-glutamyl containing substrates and is associated with several families of amidase domains. CHAP PlyC
    Protein 17
Metallopeptidase Enzymes display metallopeptidase activity; hydrolyse the peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place and charged amino acid side chains are ligands for the metal ions. Peptidase_M23 VanY LasA
Lysostaphin
Ply118
Ply500
    ZooA
  1. * in this case CHAP domain is not responsible for the main enzymatic activity of the enzybiotic.