Alpha-lytic endopeptidase

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Alpha-lytic endopeptidase
Identifiers
EC no.3.4.21.12
CAS no.37288-76-9
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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

  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. Vol. 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  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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