| EC |
3.5.1.28 |
| Accepted name: |
N-acetylmuramoyl-L-alanine amidase |
| Reaction: |
Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides |
| Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium |
| Other name(s): |
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; N-acetylmuramoyl-L-alanine amidase type II |
| Systematic name: |
peptidoglycan amidohydrolase |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9013-25-6 |
| References: |
| 1. |
Ghuysen, J.-M., Dierickx, L., Coyette, J., Leyh-Bouille, M., Guinand, M. and Campbell, J.N. An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-L-alanine amidase active on bacterial wall peptidoglycans. Biochemistry 8 (1969) 213–222. [PMID: 5777325] |
| 2. |
Herbold, D.R. and Glaser, L. Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers. J Biol Chem 250 (1975) 7231–7238. [PMID: 809432] |
| 3. |
Herbold, D.R. and Glaser, L. Bacillus subtilis N-acetylmuramic acid L-alanine amidase. J. Biol. Chem. 250 (1975) 1676–1682. [PMID: 803507] |
| 4. |
Ward, J.B., Curtis, C.A.M., Taylor, C. and Buxton, R.S. 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 (1982) 1171–1178. [DOI] [PMID: 6126517] |
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| [EC 3.5.1.28 created 1972 (EC 3.4.19.10 created 1992, incorporated 1997)] |
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