Amidase_2 |
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PFAM accession number: | PF01510 |
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Interpro abstract (IPR002502): | Proteins containing this domain include zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC 3.5.1.28 . This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The bacteriophage endolysins PLY118 and PLY500 cleave between L-Ala and D-Glu residues of Listeria cell-wall peptidoglycan and are therefore peptidases (MEROPS subfamily M15C) [ (PUBMED:8577256) ]. The structure is known for the Bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding [ (PUBMED:14506276) (PUBMED:12845326) (PUBMED:8171031) (PUBMED:15223330) (PUBMED:16556841) (PUBMED:18304640) (PUBMED:15140887) (PUBMED:16103125) (PUBMED:16428381) ]. |
GO process: | peptidoglycan catabolic process (GO:0009253) |
GO function: | N-acetylmuramoyl-L-alanine amidase activity (GO:0008745) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Amidase_2