Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase, and caseinase) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
| Lysyl endopeptidase (R) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
- Preferential cleavage: Lys-, including -Lys-Pro-
This enzyme is isolated from Lysobacter enzymogenes.
It is produced by the human body and by Achromobacter lyticus[7] that can help break down the protein casein in milk into smaller peptides and amino acids.[8]
References
edit- ^ Masaki T, Tanabe M, Nakamura K, Soejima M (July 1981). "Studies on a new proteolytic enzyme from A chromobacter lyticus M497-1. I. Purification and some enzymatic properties". Biochimica et Biophysica Acta. 660 (1): 44–50. doi:10.1016/0005-2744(81)90106-6. PMID 6791693.44-50&rft.date=1981-07&rft_id=info:doi/10.1016/0005-2744(81)90106-6&rft_id=info:pmid/6791693&rft.aulast=Masaki&rft.aufirst=T&rft.au=Tanabe, M&rft.au=Nakamura, K&rft.au=Soejima, M&rfr_id=info:sid/en.wikipedia.org:Lysyl endopeptidase" class="Z3988">
- ^ Masaki T, Fujihashi T, Nakamura K, Soejima M (July 1981). "Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. II. specificity and inhibition studies of Achromobacter protease I". Biochimica et Biophysica Acta. 660 (1): 51–5. doi:10.1016/0005-2744(81)90107-8. PMID 6168293.51-5&rft.date=1981-07&rft_id=info:doi/10.1016/0005-2744(81)90107-8&rft_id=info:pmid/6168293&rft.aulast=Masaki&rft.aufirst=T&rft.au=Fujihashi, T&rft.au=Nakamura, K&rft.au=Soejima, M&rfr_id=info:sid/en.wikipedia.org:Lysyl endopeptidase" class="Z3988">
- ^ Jekel PA, Weijer WJ, Beintema JJ (October 1983). "Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis". Analytical Biochemistry. 134 (2): 347–54. doi:10.1016/0003-2697(83)90308-1. PMID 6359954.347-54&rft.date=1983-10&rft_id=info:doi/10.1016/0003-2697(83)90308-1&rft_id=info:pmid/6359954&rft.aulast=Jekel&rft.aufirst=PA&rft.au=Weijer, WJ&rft.au=Beintema, JJ&rfr_id=info:sid/en.wikipedia.org:Lysyl endopeptidase" class="Z3988">
- ^ Elliott BW, Cohen C (August 1986). "Isolation and characterization of a lysine-specific protease from Pseudomonas aeruginosa". The Journal of Biological Chemistry. 261 (24): 11259–65. doi:10.1016/S0021-9258(18)67377-6. PMID 3090046.11259-65&rft.date=1986-08&rft_id=info:doi/10.1016/S0021-9258(18)67377-6&rft_id=info:pmid/3090046&rft.aulast=Elliott&rft.aufirst=BW&rft.au=Cohen, C&rft_id=https://doi.org/10.1016%2FS0021-9258%2818%2967377-6&rfr_id=info:sid/en.wikipedia.org:Lysyl endopeptidase" class="Z3988">
- ^ Ohara T, Makino K, Shinagawa H, Nakata A, Norioka S, Sakiyama F (December 1989). "Cloning, nucleotide sequence, and expression of Achromobacter protease I gene". The Journal of Biological Chemistry. 264 (34): 20625–31. doi:10.1016/S0021-9258(19)47109-3. PMID 2684982.20625-31&rft.date=1989-12&rft_id=info:doi/10.1016/S0021-9258(19)47109-3&rft_id=info:pmid/2684982&rft.aulast=Ohara&rft.aufirst=T&rft.au=Makino, K&rft.au=Shinagawa, H&rft.au=Nakata, A&rft.au=Norioka, S&rft.au=Sakiyama, F&rft_id=https://doi.org/10.1016%2FS0021-9258%2819%2947109-3&rfr_id=info:sid/en.wikipedia.org:Lysyl endopeptidase" class="Z3988">
- ^ Tsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F (March 1989). "The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease". The Journal of Biological Chemistry. 264 (7): 3832–9. doi:10.1016/S0021-9258(19)84926-8. PMID 2492988.3832-9&rft.date=1989-03&rft_id=info:doi/10.1016/S0021-9258(19)84926-8&rft_id=info:pmid/2492988&rft.aulast=Tsunasawa&rft.aufirst=S&rft.au=Masaki, T&rft.au=Hirose, M&rft.au=Soejima, M&rft.au=Sakiyama, F&rft_id=https://doi.org/10.1016%2FS0021-9258%2819%2984926-8&rfr_id=info:sid/en.wikipedia.org:Lysyl endopeptidase" class="Z3988">
- ^ "BRENDA - Information on EC 3.4.21.50 - lysyl endopeptidase". www.brenda-enzymes.org. Retrieved 2018-05-28.
- ^ "Caseinase Definition and Examples - Biology Online Dictionary". 7 October 2019.
External links
edit- Lysyl endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
