Endopeptidase La (EC 3.4.21.53, ATP-dependent serine proteinase, lon proteinase, protease La, proteinase La, ATP-dependent lon proteinase, ATP-dependent protease La, Escherichia coli proteinase La, Escherichia coli serine proteinase La, gene lon protease, gene lon proteins, PIM1 protease, PIM1 proteinase, serine protease La) is an enzyme.[1][2][3] This enzyme catalyses hydrolysis of proteins in the presence of ATP.
| Endopeptidase La | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.53 | ||||||||
| CAS no. | 79818-35-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme is a product of the lon gene in Escherichia coli.
References
edit- ^ Desautels M, Goldberg AL (October 1982). "Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria". The Journal of Biological Chemistry. 257 (19): 11673–9. doi:10.1016/S0021-9258(18)33815-8. PMID 6749845.
- ^ Larimore FS, Waxman L, Goldberg AL (April 1982). "Studies of the ATP-dependent proteolytic enzyme, protease La, from Escherichia coli". The Journal of Biological Chemistry. 257 (8): 4187–95. doi:10.1016/S0021-9258(18)34704-5. PMID 7040380.
- ^ Chin DT, Goff SA, Webster T, Smith T, Goldberg AL (August 1988). "Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La". The Journal of Biological Chemistry. 263 (24): 11718–28. doi:10.1016/S0021-9258(18)37843-8. PMID 3042779.
External links
edit- Endopeptidase+La at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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