Global InformationLysyl endopeptidase information
| 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 | ||||||||
| |||||||||
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
- 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]
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ "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.