Lysyl endopeptidase

Lysyl endopeptidase
Identifiers
EC number 3.4.21.50
CAS number 123175-82-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

Preferential cleavage: Lys-, including -Lys-Pro-

This enzyme is isolated from Achromobacter lyticus.

References

  1. Masaki, T.; Tanabe, M.; Nakamura, K.; Soejima, M. (1981). "Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. I. Purification and some enzymatic properties". Biochim. Biophys. Acta. 660: 44–50. doi:10.1016/0005-2744(81)90106-6. PMID 6791693.
  2. Masaki, T.; Fujihasi, T.; Nakamura, K.; Soejima, M. (1981). "Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. Specificity and inhibition studies of Achromobacter protease I". Biochim. Biophys. Acta. 660: 51–55. doi:10.1016/0005-2744(81)90107-8. PMID 6168293.
  3. Jekel, P.A.; Weijer, W.J.; Beintema, J.J. (1983). "Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis". Anal. Biochem. 134: 347–354. doi:10.1016/0003-2697(83)90308-1. PMID 6359954.
  4. Elliott, B.W.; Cohen, C. (1986). "Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa". J. Biol. Chem. 261: 11259–11265. PMID 3090046.
  5. Ohara, T.; Makino, K.; Shinagawa, H.; Nakata, A.; Norioka, S.; Sakiyama, F. (1989). "Cloning, nucleotide sequence, and expression of Achromobacter protease I gene". J. Biol. Chem. 264: 20625–2063. PMID 2684982.
  6. Tsunasawa, S.; Masaki, T.; Hirose, M.; Soejima, M.; Sakiyama, F. (1989). "The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease". J. Biol. Chem. 264: 3832–3839. PMID 2492988.
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