N-acetylmuramoyl-L-alanine amidase

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N-acetylmuramoyl-L-alanine amidase
Identifiers
EC number3.5.1.28
CAS number9013-25-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Amidase_2
PDB 1sk4 EBI.jpg
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
Identifiers
SymbolAmidase_2
PfamPF01510
InterProIPR002502
SCOPe1lba / SUPFAM
Amidase_3
PDB 1jwq EBI.jpg
structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus
Identifiers
SymbolAmidase_3
PfamPF01520
Pfam clanCL0035
InterProIPR002508
SCOPe1jwq / SUPFAM
Amidase_5
Identifiers
SymbolAmidase_5
PfamPF05382
Pfam clanCL0125
InterProIPR008044
Amidase02_C
Identifiers
SymbolAmidase02_C
PfamPF12123
InterProIPR021976

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[edit]

References[edit]

  • 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. PMID 809432.
  • Herbold DR, Glaser L (1975). "Bacillus subtilis N-acetylmuramic acid L-alanine amidase". J. Biol. Chem. 250 (5): 1676–82. 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.