| 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 | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
| Amidase_5 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Amidase_5 | ||||||||
| Pfam | PF05382 | ||||||||
| Pfam clan | CL0125 | ||||||||
| InterPro | IPR008044 | ||||||||
| |||||||||
| Amidase02_C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Amidase02_C | ||||||||
| Pfam | PF12123 | ||||||||
| InterPro | IPR021976 | ||||||||
| |||||||||
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.
- 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.
| 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 | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
| 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 | ||||||||
| |||||||||
| Amidase_5 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Amidase_5 | ||||||||
| Pfam | PF05382 | ||||||||
| Pfam clan | CL0125 | ||||||||
| InterPro | IPR008044 | ||||||||
| |||||||||
| Amidase02_C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Amidase02_C | ||||||||
| Pfam | PF12123 | ||||||||
| InterPro | IPR021976 | ||||||||
| |||||||||
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.
- 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.