Biology:Alpha-lytic endopeptidase
| Alpha-lytic endopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.12 | ||||||||
| CAS number | 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 | ||||||||
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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
- ↑ "Primary structure of alpha-lytic protease: a bacterial homologue of the pancreatic serine proteases". Nature 228 (5270): 438–42. October 1970. doi:10.1038/228438a0. PMID 5482494.
- ↑ "Structure and function of serine proteases". New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. 1987. pp. 159–200. https://www.elsevier.com/books/hydrolytic-enzymes/brocklehurst/978-0-444-80886-8.
- ↑ "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. November 1988. PMID 3053694.
- ↑ "Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates". Biochemistry 28 (19): 7600–9. September 1989. doi:10.1021/bi00445a015. PMID 2611204.
- ↑ "Expanding proteome coverage with orthogonal-specificity α-lytic proteases". Molecular & Cellular Proteomics 13 (3): 823–35. March 2014. doi:10.1074/mcp.M113.034710. PMID 24425750.
- ↑ "Site-specific identification and quantitation of endogenous SUMO modifications under native conditions" (in En). Nature Communications 8 (1): 1171. October 2017. doi:10.1038/s41467-017-01271-3. PMID 29079793.
External links
- Alpha-lytic+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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