Function and Biology Details
Reactions catalysed:
Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)(2))Asn- structure. One N-acetyl-D-glucosamine residue remains attached to the protein, the rest of the oligosaccharide is released intact.
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Bifunctional autolysin (preferred)
PDBe Complex ID:
PDB-CPX-173483 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional autolysin
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.27 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
Length: 225 amino acids
Theoretical weight: 25.27 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q2FZK7 (Residues: 198-421; Coverage: 18%)
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Peptidoglycan recognition protein-like
