Lysyl endopeptidase
Appearance
Lysyl endopeptidase | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.21.50 | ||||||||
CAS no. | 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 | ||||||||
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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
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
External links
- Lysyl+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)