Alpha-lytic endopeptidase
| Alpha-lytic endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.12 | ||||||||
| CAS number | 37288-76-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Alpha-lytic endopeptidase (EC 3.4.21.12, myxobacter alpha-lytic proteinase, alpha-lytic proteinase, alpha-lytic protease, Mycobacterium sorangium alpha-lytic proteinase, Myxobacter 495 alpha-lytic proteinase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Preferential cleavage: Ala-, Val- in bacterial cell walls, elastin and other proteins
This enzyme is isolated from the myxobacterium Lysobacter enzymogenes.
References
- ↑ Olson, M.O.J.; Nagabushan, N.; Dzwiniel, M.; Smillie, L.B.; Whitaker, D.R. (1970). "Primary structure of α-lytic protease: a bacterial homologue of the pancreatic serine proteases". Nature. 228: 438–442. doi:10.1038/228438a0. PMID 5482494.
- ↑ Polgar, L. (1987). "Structure and function of serine proteases". In Neuberger, A.; Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. pp. 159–200.
- ↑ Epstein, D.M.; Wensink, P.C. (1988). "The α-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes". J. Biol. Chem. 263: 16586–16590. PMID 3053694.
- ↑ Bone, R.; Frank, D.; Kettner, C.A.; Agard, D.A. (1989). "Structural analysis of specificity: α-lytic protease complexes with analogues of reaction intermediates". Biochemistry. 28: 7600–7609. doi:10.1021/bi00445a015. PMID 2611204.
External links
- Alpha-lytic endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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