220.127.116.11: alpha-lytic endopeptidase
This is an abbreviated version, for detailed information about alpha-lytic endopeptidase, go to the full flat file.
preferential cleavage: Ala-/-, Val-/- in bacterial cell walls, elastin and other proteins
ALP, Alpha-lytic endopeptidase, alpha-lytic protease, alpha-lytic proteinase, alphaLP, Mycobacterium sorangium alpha-lytic proteinase, Myxobacter 495 alpha-lytic proteinase, Myxobacter alpha-lytic proteinase, proteinase, Mycobacterium sorangium alpha-lytic, proteinase, Myxobacter alpha-lytic
Posttranslational Modification on EC 18.104.22.168 - alpha-lytic endopeptidase
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the enzyme is synthesized with a large, two-domain pro region (Pro) that catalyzes the folding of the protease to its native conformation. In the absence of its (Pro) folding catalyst, alpha-lytic protease encounters a very large folding barrier that effectively prevents the protease from folding. The extremely high alpha-lytic protease folding barrier necessitates the presence of both the (Pro) domains
the enzyme is synthesized with a 166 amino acid pro region that catalyzes the folding of the 198 amino acid protease into its native conformation.