Alpha-lytic endopeptidase
| Alpha-lytic endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.12 | ||||||||
| CAS no. | 37288-76-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Alpha-lytic endopeptidase or Alpha-lytic protease (EC 3.4.21.12, myxobacter alpha-lytic proteinase, alpha-lytic proteinase, alpha-lytic protease, Mycobacterium sorangium alpha-lytic proteinase, Myxobacter 495 alpha-lytic proteinase) is an enzyme isolated from the myxobacterium Lysobacter enzymogenes.[1][2][3][4] This enzyme is a serine protease that catalyses the breakage of peptide bonds using a hydrolysis chemical reaction. Alpha-lytic protease was named based on the observed cleavage specificity for the α position of the tetrapeptide component in gram-positive bacterial cell walls (alanine). Alpha-lytic protease is also capable of digesting elastin and other proteins.
This protease was recently applied to proteome digestion for production of peptides for mass spectrometry-based proteomics,[5] where it was found to cleave preferentially after several small amino acids, including alanine, serine, threonine, valine, and to a lesser extent, methionine. This specificity is very different than the most commonly-used protease for proteomics, trypsin, which cleaves only after arginine and lysine.
Alpha-lytic protease was also recently reported to find utility as part of a method to map endogenous SUMO modification sites in the proteome.[6]
References
[edit]- ^ Olson MO, Nagabhushan N, Dzwiniel M, Smillie LB, Whitaker DR (October 1970). "Primary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases". Nature. 228 (5270): 438–42. Bibcode:1970Natur.228..438O. doi:10.1038/228438a0. PMID 5482494.
- ^ Polgar L (1987). "Structure and function of serine proteases". In Neuberger A, Brocklehurst K (eds.). New Comprehensive Biochemistry: Hydrolytic Enzymes. Vol. 16. Amsterdam: Elsevier. pp. 159–200.
- ^ Epstein DM, Wensink PC (November 1988). "The alpha-lytic protease gene of Lysobacter enzymogenes. The nucleotide sequence predicts a large prepro-peptide with homology to pro-peptides of other chymotrypsin-like enzymes". The Journal of Biological Chemistry. 263 (32): 16586–90. doi:10.1016/S0021-9258(18)37430-1. PMID 3053694.
- ^ Bone R, Frank D, Kettner CA, Agard DA (September 1989). "Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates". Biochemistry. 28 (19): 7600–9. doi:10.1021/bi00445a015. PMID 2611204.
- ^ Meyer JG, Kim S, Maltby DA, Ghassemian M, Bandeira N, Komives EA (March 2014). "Expanding proteome coverage with orthogonal-specificity α-lytic proteases". Molecular & Cellular Proteomics. 13 (3): 823–35. doi:10.1074/mcp.M113.034710. PMC 3945911. PMID 24425750.
- ^ Lumpkin RJ, Gu H, Zhu Y, Leonard M, Ahmad AS, Clauser KR, Meyer JG, Bennett EJ, Komives EA (October 2017). "Site-specific identification and quantitation of endogenous SUMO modifications under native conditions". Nature Communications. 8 (1): 1171. Bibcode:2017NatCo...8.1171L. doi:10.1038/s41467-017-01271-3. PMC 5660086. PMID 29079793.
External links
[edit]- Alpha-lytic+endopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
