Desampylase
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.19 Omega peptidases > 3.4.19.15 desampylase
Desampylase is a zinc-containing isopeptidase characterised from the archaeon Haloferax volcanii that specifically cleaves the ubiquitin-like small archaeal modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolysing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier (cf. ubiquitinyl hydrolase 1 EC 3.4.19.12); it is in peptidase family M67 and hydrolyses an N6-[small archaeal modifier protein]-[protein]-L-lysine plus water into [protein]-L-lysine and the free modifier. By removing SAMP modifiers it reverses archaeal ubiquitin-like protein conjugation.
Desampylase is a zinc-containing isopeptidase characterised from the archaeon Haloferax volcanii that specifically cleaves the ubiquitin-like small archaeal modifier proteins SAMP1 and SAMP2 from protein conjugates, hydrolysing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier (cf. ubiquitinyl hydrolase 1 EC 3.4.19.12); it is in peptidase family M67 and hydrolyses an N6-[small archaeal modifier protein]-[protein]-L-lysine plus water into [protein]-L-lysine and the free modifier. By removing SAMP modifiers it reverses archaeal ubiquitin-like protein conjugation.
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