Lysyl endopeptidase
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. and 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. and 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. and 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. and 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. and 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. and 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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