N-acetylmuramoyl-L-alanine amidase

N-acetylmuramoyl-L-alanine amidase
Identifiers
EC no.	3.5.1.28
CAS no.	9013-25-6
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

Amidase_2
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
Identifiers
Symbol	Amidase_2
Pfam	PF01510
InterPro	IPR002502
SCOP2	1lba / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Amidase_3
structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus
Identifiers
Symbol	Amidase_3
Pfam	PF01520
Pfam clan	CL0035
InterPro	IPR002508
SCOP2	1jwq / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Amidase_5
Identifiers
Symbol	Amidase_5
Pfam	PF05382
Pfam clan	CL0125
InterPro	IPR008044
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Amidase02_C
Identifiers
Symbol	Amidase02_C
Pfam	PF12123
InterPro	IPR021976
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, a N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) is an enzyme that catalyzes a chemical reaction that cleaves the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L-alanine amidase, N-acetylmuramyl-L-alanine amidase, N-acylmuramyl-L-alanine amidase, acetylmuramoyl-alanine amidase, N-acetylmuramic acid L-alanine amidase, acetylmuramyl-alanine amidase, N-acetylmuramylalanine amidase, N-acetylmuramoyl-L-alanine amidase type I, and N-acetylmuramoyl-L-alanine amidase type II. This enzyme participates in peptidoglycan biosynthesis. Autolysins and some phage lysins are examples of N-acetylmuramoyl-L-alanine amidases.

See also

• Phage lysins
• Autolysins
• PGLYRP2

References

• Campbell JN; Dierickx, L; Coyette, J; Leyh-Bouille, M; Guinand, M; Campbell, JN (1969). "An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-l-alanine amidase active on bacterial wall peptidoglycans". Biochemistry. 8 (1): 213–22. doi:10.1021/bi00829a031. PMID 5777325.
• Herbold DR, Glaser L (1975). "Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers". J. Biol. Chem. 250 (18): 7231–8. doi:10.1016/S0021-9258(19)40933-2. PMID 809432.
• Herbold DR, Glaser L (1975). "Bacillus subtilis N-acetylmuramic acid L-alanine amidase". J. Biol. Chem. 250 (5): 1676–82. doi:10.1016/S0021-9258(19)41746-8. PMID 803507.
• Ward JB, Curtis CA, Taylor C, Buxton RS (1982). "Purification and characterization of two phage PBSX-induced lytic enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine amidase and an N-acetylmuramidase". J. Gen. Microbiol. 128 (6): 1171–8. doi:10.1099/00221287-128-6-1171. PMID 6126517.