Table 2.
Characterisation of proposed phiBIOTICS families of enzybiotics
| 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 |
* in this case CHAP domain is not responsible for the main enzymatic activity of the enzybiotic.