Lysyl endopeptidase - Misplaced Pages

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. 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 that can help break down the protein casein in milk into smaller peptides and amino acids.

References

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.

External links

Lysyl+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.4.21