| EC |
3.4.19.15 |
| Accepted name: |
desampylase |
| Reaction: |
an N6-[small archaeal modifier protein]-[protein]-L-lysine + H2O = a [protein]-L-lysine + a small archaeal modifier protein |
| Glossary: |
SAMP = small archaeal modifier protein |
| Other name(s): |
SAMP-protein conjugate cleaving protease; HvJAMM1 |
| Systematic name: |
N6-[small archaeal modifier protein]-[protein]-L-lysine hydrolase |
| Comments: |
The enzyme, characterized from the archaeon Haloferax volcanii, specifically cleaves the ubiquitin-like small 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 protein. The enzyme contains Zn2+. cf. EC 3.4.19.12, ubiquitinyl hydrolase 1. In peptidase family M67. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB |
| References: |
| 1. |
Hepowit, N.L., Uthandi, S., Miranda, H.V., Toniutti, M., Prunetti, L., Olivarez, O., De Vera, I.M., Fanucci, G.E., Chen, S. and Maupin-Furlow, J.A. Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like small archaeal modifier proteins (SAMPs) from protein-conjugates. Mol. Microbiol. 86 (2012) 971–987. [DOI] [PMID: 22970855] |
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| [EC 3.4.19.15 created 2015 as EC 3.4.24.88, transferred 2016 to EC 3.4.19.15] |
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