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

  1. Olson, M.O.J., Nagabushan, N., Dzwiniel, M., Smillie, L.B. and 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.
  2. Polgár, L. (1987). "Structure and function of serine proteases". In Neuberger, A. and Brocklehurst, K. New Comprehensive Biochemistry: Hydrolytic Enzymes 16. Amsterdam: Elsevier. pp. 159–200.
  3. Epstein, D.M. and 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.
  4. Bone, R., Frank, D., Kettner, C.A. and 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

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