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
^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. PMID5482494.
^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. PMID2611204.
