- N-acetylmuramoyl-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase Identifiers EC number 3.5.1.28 CAS number 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 / EGO Search PMC articles PubMed articles 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 SCOP 1lba Available protein structures: Pfam structures PDB RCSB PDB; PDBe 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 SCOP 1jwq Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary Amidase_5 Identifiers Symbol Amidase_5 Pfam PF05382 Pfam clan CL0125 InterPro IPR008044 Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary Amidase02_C Identifiers Symbol Amidase02_C Pfam PF12123 InterPro IPR021976 Available protein structures: Pfam structures PDB RCSB PDB; PDBe 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, murein hydrolase, N-acetylmuramoyl-L-alanine amidase type I, and N-acetylmuramoyl-L-alanine amidase type II. This enzyme participates in peptidoglycan biosynthesis.
Structural studies
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1ARO, 1GVM, 1H8G, 1HCX, 1J3G, 1JWQ, 1LBA, 1X60, 1XOV, 2AR3, 2BGX, 2BH7, and 2BML.
See also
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. 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. PMID 6126517.
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