Alpha-lytic endopeptidase

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.

Alpha-lytic endopeptidase
Identifiers
EC number3.4.21.12
CAS number37288-76-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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
  1. 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. doi:10.1038/228438a0. PMID 5482494.
  2. Polgar L (1987). "Structure and function of serine proteases". In Neuberger A, Brocklehurst K (eds.). New Comprehensive Biochemistry: Hydrolytic Enzymes. 16. Amsterdam: Elsevier. pp. 159–200.
  3. 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. PMID 3053694.
  4. 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.
  5. 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.
  6. 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. doi:10.1038/s41467-017-01271-3. PMC 5660086. PMID 29079793.
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