Table 2 Characterisation of proposed phiBIOTICS families of enzybiotics

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